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Entry Information
Entry status
(1)
Experimental methods
(2)
X-ray diffraction
(153)
Electron Microscopy
(6)
Authors
(333)
Christianson DW
(94)
Ash DE
(34)
Hai Y
(28)
Di Costanzo L
(26)
Emig FA
(25)
Cama E
(24)
Van Zandt MC
(21)
Gathiaka S
(20)
Palte RL
(20)
Miller JR
(18)
D'Antonio EL
(17)
Fischer C
(14)
Chakravarthy K
(13)
Ilies M
(13)
Li D
(13)
O'Neil J
(13)
Beard A
(12)
Cox JD
(12)
Kim HY
(12)
Lyons TW
(12)
Palani A
(12)
Sauri J
(12)
Saurí J
(12)
Sloman DL
(12)
Zhang H
(12)
Cousido-Siah A
(11)
Han S
(11)
Mitschler A
(11)
Scolnick LR
(11)
Viola RE
(11)
Colleluori DM
(10)
Edwards JE
(10)
Golebiowski A
(10)
Hoffmann KF
(10)
Kanyo ZF
(10)
Achab A
(9)
Andreoli M
(9)
Beckett P
(9)
Ji MK
(9)
Lesburg CA
(9)
Martinot TA
(9)
Mitcheltree MJ
(9)
Podjarny A
(9)
Ruiz FX
(9)
Ryder TR
(9)
Schroeter H
(9)
Thorn KJ
(9)
Wang J
(9)
Boucher JL
(8)
Childers M
(8)
Cumming J
(8)
Lu M
(8)
Mansuy D
(8)
Pethe S
(8)
Pu Q
(8)
Spacciapoli P
(8)
Cheng M
(7)
Cho H
(7)
Dowling DP
(7)
Eangoor P
(7)
Aquila BM
(6)
Bailly MA
(6)
Barrett MP
(6)
Beckett RP
(6)
Chen X
(6)
Cipriano D
(6)
Compher K
(6)
Conway B
(6)
Fayad GN
(6)
Fayadat-Dilman L
(6)
Finlay MRV
(6)
Gangl ET
(6)
Gomez-Llorente Y
(6)
Greb H
(6)
Gu C
(6)
Hall B
(6)
Handa M
(6)
Howard EI
(6)
Hsieh M
(6)
Jagdmann GE
(6)
Ji M
(6)
Juan V
(6)
Jude K
(6)
Kerkhoven EJ
(6)
Kofman E
(6)
Lin H
(6)
Mlynarski SN
(6)
Nguyen N
(6)
Petersen J
(6)
Podjarny AD
(6)
Pop-Damkov P
(6)
Reczkowski RS
(6)
Scapin G
(6)
Shaheen H
(6)
Sheeler R
(6)
Shields JD
(6)
Simpson I
(6)
Sterner E
(6)
Strickland C
(6)
Sun A
(6)
More...
Homo / hetero assembly
(2)
homo
(149)
hetero
(10)
Assembly composition
(2)
protein structure
(149)
protein/protein complex
(10)
Assembly polymer count
(8)
trimer
(119)
monomer
(14)
hexamer
(11)
dimer
(5)
nonamer
(4)
octadecamer
(4)
octamer
(1)
tetradecamer
(1)
Resolution distribution
1.0 - 1.5
(9)
1.5 - 2
(63)
2.0 - 2.5
(51)
2.5 - 3
(26)
3.0 - 3.5
(5)
3.5 - 4
(3)
4.0 - 4.5
(2)
Release year distribution
1995 - 2000
(11)
2000 - 2005
(29)
2005 - 2010
(36)
2010 - 2015
(55)
2015 - 2020
(25)
2020 - 2025
(34)
Journal
(22)
Biochemistry
(54)
J Med Chem
(20)
Arch Biochem Biophys
(15)
ACS Med Chem Lett
(12)
To be published
(10)
Bioorg Med Chem Lett
(7)
Commun Biol
(6)
J Am Chem Soc
(6)
Structure
(5)
FEBS J
(3)
Front Plant Sci
(3)
J Struct Biol X
(3)
Proc Natl Acad Sci U S A
(3)
Acta Crystallogr F Struct Biol Commun
(2)
Acta Crystallogr Sect F Struct Biol Cryst Commun
(2)
MAbs
(2)
J Biol Chem
(1)
Mol Cancer Ther
(1)
Nat Struct Biol
(1)
Nature
(1)
Org Biomol Chem
(1)
Traffic
(1)
Macromolecules
Organism name
(18)
Homo sapiens
(78)
Rattus norvegicus
(34)
Schistosoma mansoni
(10)
Leishmania mexicana
(7)
Trypanosoma brucei brucei TREU927
(6)
[Bacillus] caldovelox
(5)
Entamoeba histolytica
(3)
Plasmodium falciparum 3D7
(3)
Bacillus subtilis subsp. subtilis str. 168
(2)
Glaciozyma antarctica
(2)
Medicago truncatula
(2)
Thermus thermophilus
(2)
Arabidopsis thaliana
(1)
Bacillus thuringiensis DB27
(1)
Fusobacterium nucleatum subsp. nucleatum ATCC 25586
(1)
Helicobacter pylori 26695
(1)
Mus musculus
(1)
Thermus thermophilus HB8
(1)
Molecule name
(33)
Arginase-1
(94)
Liver-type arginase
(94)
Type I arginase
(94)
Arginase
(37)
Arginase II
(18)
Arginase-2, mitochondrial
(18)
Kidney-type arginase
(18)
Non-hepatic arginase
(18)
Type II arginase
(18)
Arginase, putative
(6)
EhArg
(3)
PFA
(3)
PfArg
(3)
Agmatinase ARGAH
(2)
Arginase, mitochondrial
(2)
Arginine amidohydrolase
(2)
MtARGAH
(2)
Agmatinase ARGAH1
(1)
Arginase (RocF)
(1)
Arginase 1, mitochondrial
(1)
Arginine amidohydrolase 1
(1)
AtARGAH1
(1)
Importin alpha P1
(1)
Importin subunit alpha-1
(1)
Karyopherin subunit alpha-2
(1)
Ornithine decarboxylase
(1)
PTAC58
(1)
Pendulin
(1)
Pore targeting complex 58 kDa subunit
(1)
RAG cohort protein 1
(1)
SRP1-alpha
(1)
Uncharacterized protein
(1)
arginase
(1)
Molecule type
(1)
Protein
(159)
Gene names
(22)
ARG1
(60)
Arg1
(34)
ARG2
(18)
ARG
(13)
rocF
(7)
Tb08.26N11.490
(6)
Tb927.8.2020
(6)
EHI_152330
(3)
PF3D7_0906500
(3)
TTHA1496
(3)
ARGAH
(2)
BSU40320
(2)
MTR_4g024960
(2)
MtrunA17_Chr4g0011501
(2)
ARGAH1
(1)
At4g08900
(1)
BTDB27_005763
(1)
FN0501
(1)
HP_1399
(1)
Kpna2
(1)
Rch1
(1)
T3H13.7
(1)
Interacting Molecules
(17)
mAb1 heavy chain
(2)
mAb1 light chain
(2)
DNA nucleotidylexotransferase
(1)
Fab C0020187 heavy chain (IgG1)
(1)
Fab C0020187 light chain (IgG1)
(1)
Fab C0021158 heavy chain (IgG1)
(1)
Fab C0021158 light chain (IgG1)
(1)
Fab C0021181 heavy chain (IgG1)
(1)
Fab C0021181 light chain (IgG1)
(1)
mAb2 heavy chain
(1)
mAb2 light chain
(1)
mAb3 heavy chain
(1)
mAb3 light chain
(1)
mAb4 monoclonal antibody heavy chain
(1)
mAb4 monoclonal antibody light chain
(1)
mAb5 heavy chain
(1)
mAb5 light chain
(1)
Interacting ligands
(83)
MN : MANGANESE (II) ION
(138)
GOL : GLYCEROL
(30)
ABH : 2(S)-AMINO-6-BORONOHEXANOIC ACID
(14)
BME : BETA-MERCAPTOETHANOL
(10)
EDO : 1,2-ETHANEDIOL
(10)
ORN : L-ornithine
(9)
BEN : BENZAMIDINE
(8)
S2C : S-2-(BORONOETHYL)-L-CYSTEINE
(8)
SO4 : SULFATE ION
(6)
CO : COBALT (II) ION
(5)
NA : SODIUM ION
(5)
CL : CHLORIDE ION
(4)
GAI : GUANIDINE
(4)
HAR : N-OMEGA-HYDROXY-L-ARGININE
(4)
LYS : LYSINE
(4)
NNH : NOR-N-OMEGA-HYDROXY-L-ARGININE
(4)
X7A : [(5R)-5-amino-5-carboxy-7-(piperidin-1-yl)heptyl](trihydroxy)borate(1-)
(4)
ZN : ZINC ION
(3)
1EC : [(5R)-5-amino-5-carboxy-8-hydroxyoctyl](trihydroxy)borate(1-)
(2)
ARG : ARGININE
(2)
GPA : 2-AMINO-3-GUANIDINO-PROPIONIC ACID
(2)
NI : NICKEL (II) ION
(2)
PEG : DI(HYDROXYETHYL)ETHER
(2)
PGE : TRIETHYLENE GLYCOL
(2)
URE : UREA
(2)
VAL : VALINE
(2)
X8A : [(5R)-5-carboxy-5-(methylamino)-7-(piperidin-1-yl)heptyl](trihydroxy)borate(1-)
(2)
XA2 : (R)-2-amino-6-borono-2-(1-(3,4-dichlorobenzyl)piperidin-4-yl)hexanoic acid
(2)
0IZ : 3-[(2~{S},3~{R},4~{R})-4-[[(2~{S})-2-azanyl-3-methyl-butanoyl]amino]-2-carboxy-pyrrolidin-3-yl]propyl-$l^{3}-oxidanyl-bis(oxidanyl)boron
(1)
1EE : [(5R)-5-amino-5-carboxy-7-(4-hydroxypiperidin-1-yl)heptyl](trihydroxy)borate(1-)
(1)
2AI : 1H-imidazol-2-amine
(1)
2BH : [(1E,5S)-5-AMINO-5-CARBOXYPENT-1-ENYL](TRIHYDROXY)BORATE(1-)
(1)
38I : {(5R)-5-amino-5-carboxy-5-[(3-endo)-8-(3,4-dichlorobenzyl)-8-azabicyclo[3.2.1]oct-3-yl]pentyl}(trihydroxy)borate(1-)
(1)
4U7 : [(5S)-5-amino-5-carboxy-6,6-difluorohexyl](trihydroxy)borate(1-)
(1)
5AB : [(5S)-5-amino-5-carboxyhexyl](trihydroxy)borate
(1)
6HN : 6-nitro-L-norleucine
(1)
A1H04 : [(5~{S})-5-azanyl-4-[[[(2~{S})-2-azanyl-3-methyl-butanoyl]amino]methyl]-6-oxidanyl-6-oxidanylidene-hexyl]-$l^{3}-oxidanyl-bis(oxidanyl)boron
(1)
A1H0A : 4-[(2~{R},4~{R})-4-azanyl-2-carboxy-pyrrolidin-2-yl]butyl-tris(oxidanyl)boranuide
(1)
A1H0B : (2~{S},3~{R})-3-[3-(dihydroxyboranyl)propyl]pyrrolidine-2-carboxylic acid
(1)
A1HZ9 : [(4~{R},5~{S})-4-(aminomethyl)-5-azanyl-6-oxidanyl-6-oxidanylidene-hexyl]-tris(oxidanyl)boron
(1)
A1IFX : [(4~{S},5~{S})-4-(aminomethyl)-5-azanyl-6-oxidanyl-6-oxidanylidene-hexyl]-$l^{3}-oxidanyl-bis(oxidanyl)boron
(1)
AHI : 3-{[(E)-AMINO(HYDROXYIMINO)METHYL]AMINO}PROPAN-1-AMINIUM
(1)
B3U : 2-amino-L-histidine
(1)
BCN : BICINE
(1)
CA : CALCIUM ION
(1)
CS : CESIUM ION
(1)
DHH : (S)-2-AMINO-7,7-DIHYDROXYHEPTANOIC ACID
(1)
DIR : 3-{[(E)-AMINO(HYDROXYIMINO)METHYL]AMINO}ALANINE
(1)
DMO : ALPHA-DIFLUOROMETHYLORNITHINE
(1)
DMS : DIMETHYL SULFOXIDE
(1)
EXY : 6-[(2R)-oxiran-2-yl]-L-norleucine
(1)
F : FLUORIDE ION
(1)
FB5 : 2-(difluoromethyl)-6-(dihydroxyboranyl)-L-norleucine
(1)
FB6 : 6-(dihydroxyboranyl)-2-methyl-L-norleucine
(1)
FMT : FORMIC ACID
(1)
GOA : GLYCOLIC ACID
(1)
HDQ : 3-[(3~{S},4~{R})-4-azanyl-4-carboxy-1-[[(2~{S})-piperidin-2-yl]methyl]pyrrolidin-3-yl]propyl-tris(oxidanyl)boranuide
(1)
HE8 : 3-[(3~{S},4~{R})-4-azanyl-4-carboxy-pyrrolidin-3-yl]propyl-tris(oxidanyl)boranuide
(1)
IMD : IMIDAZOLE
(1)
MG : MAGNESIUM ION
(1)
MPD : (4S)-2-METHYL-2,4-PENTANEDIOL
(1)
NVA : NORVALINE
(1)
O93 : 2-[(1~{R},3~{R},4~{S})-3-azanyl-3-carboxy-4-[(dimethylamino)methyl]cyclohexyl]ethyl-$l^{3}-oxidanyl-bis(oxidanyl)boron
(1)
PO4 : PHOSPHATE ION
(1)
PRO : PROLINE
(1)
QR1 : {3-[(3aR,4S,5S,6aR)-5-azaniumyl-5-carboxyoctahydrocyclopenta[c]pyrrol-2-ium-4-yl]propyl}(trihydroxy)borate(1-)
(1)
QR4 : {3-[(3aR,4R,5S,6aR)-4-azaniumyl-4-carboxyoctahydrocyclopenta[b]pyrrol-1-ium-5-yl]propyl}(trihydroxy)borate(1-)
(1)
QRA : 3-[(5~{S},7~{S},8~{S})-8-azanyl-8-carboxy-1-azaspiro[4.4]nonan-7-yl]propyl-$l^{3}-oxidanyl-bis(oxidanyl)boranuide
(1)
QRJ : {3-[(5R,7S,8S)-8-azaniumyl-8-carboxy-2-azaspiro[4.4]nonan-2-ium-7-yl]propyl}(trihydroxy)borate(1-)
(1)
SDC : S-[2-(AMINOSULFONYL)ETHYL]-D-CYSTEINE
(1)
TSZ : HYDRAZINECARBOTHIOAMIDE
(1)
UKR : 1-{[(3S,4S)-3-({4-[2-(4-fluorobenzene-1-sulfonyl)ethyl]piperidin-1-yl}methyl)-4-(3-fluorophenyl)pyrrolidin-1-yl]methyl}cyclopentane-1-carboxylic acid
(1)
UL0 : 1-{[(3S,4S)-3-(3-fluorophenyl)-4-{[4-(1,3,4-triethyl-1H-pyrazol-5-yl)piperidin-1-yl]methyl}pyrrolidin-1-yl]methyl}cyclopentane-1-carboxylic acid
(1)
VUS : 3-[(3~{a}~{S},4~{S},6~{a}~{R})-4-carboxy-2,3,4,5,6,6~{a}-hexahydro-1~{H}-pyrrolo[2,3-c]pyrrol-3~{a}-yl]propyl-$l^{3}-oxidanyl-bis(oxidanyl)boranuide
(1)
VUV : 3-[(2~{S},3~{R})-2-carboxypyrrolidin-3-yl]propyl-$l^{3}-oxidanyl-bis(oxidanyl)boranuide
(1)
VUY : 3-[(1~{S},2~{S},5~{R})-2-carboxy-6-thia-3-azabicyclo[3.2.0]heptan-1-yl]propyl-$l^{3}-oxidanyl-bis(oxidanyl)boranuide
(1)
VV1 : 3-[(1~{S},2~{S},5~{R})-2-carboxy-3,6-diazabicyclo[3.2.0]heptan-1-yl]propyl-$l^{3}-oxidanyl-bis(oxidanyl)boranuide
(1)
VV4 : 3-[(1~{R},5~{S},8~{R})-5-carboxy-2,6-diazabicyclo[3.2.1]octan-8-yl]propyl-$l^{3}-oxidanyl-bis(oxidanyl)boranuide
(1)
XA1 : {(5R)-5-amino-5-carboxy-5-[1-(4-chlorobenzyl)piperidin-4-yl]pentyl}(trihydroxy)borate(1-)
(1)
XC3 : [(~{E})-3-[(3~{S},4~{R})-4-azanyl-1-[(2~{S})-2-azanylpropanoyl]-4-carboxy-pyrrolidin-3-yl]prop-1-enyl]-tris(oxidanyl)boranium
(1)
XFG : 3-[(2~{S},3~{R},4~{R})-4-azanyl-2-carboxy-pyrrolidin-3-yl]propyl-$l^{3}-oxidanyl-bis(oxidanyl)boron
(1)
XFP : 3-[(2~{S},3~{R})-2-carboxypiperidin-3-yl]propyl-$l^{3}-oxidanyl-bis(oxidanyl)boranuide
(1)
Z70 : (2S)-2-amino-4-(2-amino-1H-imidazol-5-yl)butanoic acid
(1)
Function and Biology
EC number / name
(2)
3.5.3.1 : Arginase
(159)
3.5.3.11 : Agmatinase
(3)
Biological function
(11)
arginase activity
(158)
metal ion binding
(158)
hydrolase activity
(148)
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
(142)
manganese ion binding
(139)
protein binding
(69)
identical protein binding
(40)
agmatinase activity
(9)
cobalt ion binding
(1)
magnesium ion binding
(1)
nuclear import signal receptor activity
(1)
Biological process
(67)
arginine metabolic process
(158)
urea cycle
(138)
adaptive immune response
(103)
immune system process
(103)
innate immune response
(103)
defense response to protozoan
(94)
negative regulation of T cell proliferation
(94)
negative regulation of T-helper 2 cell cytokine production
(94)
negative regulation of activated T cell proliferation
(94)
negative regulation of type II interferon-mediated signaling pathway
(94)
positive regulation of neutrophil mediated killing of fungus
(94)
regulation of cell population proliferation
(94)
response to nematode
(94)
L-arginine catabolic process
(61)
cellular response to dexamethasone stimulus
(34)
cellular response to glucagon stimulus
(34)
cellular response to hydrogen peroxide
(34)
cellular response to interleukin-4
(34)
cellular response to lipopolysaccharide
(34)
cellular response to transforming growth factor beta stimulus
(34)
collagen biosynthetic process
(34)
female pregnancy
(34)
liver development
(34)
lung development
(34)
mammary gland involution
(34)
maternal process involved in female pregnancy
(34)
positive regulation of endothelial cell proliferation
(34)
regulation of L-arginine import across plasma membrane
(34)
response to amine
(34)
response to amino acid
(34)
response to axon injury
(34)
response to cadmium ion
(34)
response to herbicide
(34)
response to lipopolysaccharide
(34)
response to manganese ion
(34)
response to methylmercury
(34)
response to peptide hormone
(34)
response to selenium ion
(34)
response to steroid hormone
(34)
response to vitamin A
(34)
response to vitamin E
(34)
response to xenobiotic stimulus
(34)
response to zinc ion
(34)
negative regulation of CD4-positive, alpha-beta T cell proliferation
(9)
negative regulation of activated CD8-positive, alpha-beta T cell apoptotic process
(9)
negative regulation of chemokine (C-C motif) ligand 4 production
(9)
negative regulation of chemokine (C-C motif) ligand 5 production
(9)
negative regulation of defense response to bacterium
(9)
negative regulation of interleukin-13 production
(9)
negative regulation of interleukin-17 production
(9)
negative regulation of macrophage inflammatory protein 1 alpha production
(9)
negative regulation of multicellular organismal process
(9)
negative regulation of tumor necrosis factor production
(9)
negative regulation of type 2 immune response
(9)
nitric oxide biosynthetic process
(9)
positive regulation of cellular senescence
(9)
putrescine biosynthetic process from arginine, via agmatine
(9)
regulation of interleukin-1 beta production
(9)
regulation of reactive oxygen species biosynthetic process
(9)
striated muscle contraction
(9)
ureteric bud development
(9)
protein hexamerization
(3)
putrescine biosynthetic process
(3)
putrescine biosynthetic process from arginine
(3)
symbiont-mediated suppression of host innate immune response
(3)
glutamine family amino acid metabolic process
(2)
protein import into nucleus
(1)
Biological cell component
(11)
cytoplasm
(140)
cytosol
(119)
extracellular space
(94)
nucleus
(78)
azurophil granule lumen
(60)
extracellular region
(60)
specific granule lumen
(60)
neuronal cell body
(34)
mitochondrion
(18)
mitochondrial matrix
(9)
kinetoplast
(6)
Sequence and Structure classification
SCOP fold
(1)
Arginase/deacetylase
(45)
SCOP family
(1)
Arginase-like amidino hydrolases
(45)
CATH class
(1)
Alpha Beta
(115)
Representative Structures
Representative Structures
Entries
Macromolecules
Compounds
Protein families
...
Entries 1 to 10 of 159
Select all entries on this page
Structure of hARG1 with a novel inhibitor.
Napiorkowska-Gromadzka A, Nowak E, Nowotny M
Mol Cancer Ther
(2023)
[PMID: 36939275 ]
Source organism: Homo sapiens
Assembly composition: protein only structure
Assembly name:
Arginase-1
(Preferred)
search this complex
PDBe complex ID:
PDB-CPX-138411 (Preferred)
search this ID

Structure of ARG1 complex with pyrrolidine-based non-boronic acid inhibitor 10
Palte RL, Gathiaka S
Bioorg Med Chem Lett
(2023)
[PMID: 36822300 ]
Source organism: Homo sapiens
Assembly composition: protein only structure
Assembly name:
Arginase-1
(Preferred)
search this complex
PDBe complex ID:
PDB-CPX-138411 (Preferred)
search this ID

Structure of ARG1 complex with pyrrolidine-based non-boronic acid inhibitor 6
Palte RL, Gathiaka S
Bioorg Med Chem Lett
(2023)
[PMID: 36822300 ]
Source organism: Homo sapiens
Assembly composition: protein only structure
Assembly name:
Arginase-1
(Preferred)
search this complex
PDBe complex ID:
PDB-CPX-138411 (Preferred)
search this ID

Arginase Domain of Ornithine Decarboxylase/Arginase from Fusobacterium nucleatum
Chan AC, Kolesnikov M, Murphy ME
Biochemistry
(2022)
[PMID: 35732022 ]
Source organism: Fusobacterium nucleatum subsp. nucleatum ATCC 25586
Assembly composition: protein only structure
Assembly name:
arginase
(Preferred)
search this complex
PDBe complex ID:
PDB-CPX-275188 (Preferred)
search this ID

Arginase 2 in complex with inhibitor
Petersen j
J Med Chem
(2024)
[PMID: 39540340 ]
Source organism: Homo sapiens
Assembly composition: protein only structure
Assembly name:
Arginase-2, mitochondrial
(Preferred)
search this complex
PDBe complex ID:
PDB-CPX-160277 (Preferred)
search this ID

Arginase 2 in complex with inhibitor
Petersen J
J Med Chem
(2024)
[PMID: 39572889 ]
Source organism: Homo sapiens
Assembly composition: protein only structure
Assembly name:
Arginase-2, mitochondrial
(Preferred)
search this complex
PDBe complex ID:
PDB-CPX-160277 (Preferred)
search this ID

Arginase 2 in complex with an inhibitor
Petersen J
J Med Chem
(2024)
[PMID: 39572889 ]
Source organism: Homo sapiens
Assembly composition: protein only structure
Assembly name:
Arginase-2, mitochondrial
(Preferred)
search this complex
PDBe complex ID:
PDB-CPX-160277 (Preferred)
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1.7 Angstrom Resolution Crystal Structure of Arginase from Bacillus subtilis subsp. subtilis str. 168
Minasov G, Wawrzak Z, Evdokimova E, Grimshaw S, Kwon K, Savchenko A, Satchell KJF, Joachimiak A, Center for Structural Genomics of Infectious Diseases (CSGID)
To be published
Source organism: Bacillus subtilis subsp. subtilis str. 168
Assembly composition: protein only structure
Assembly name:
Arginase
(Preferred)
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PDBe complex ID:
PDB-CPX-153845 (Preferred)
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Human Arginase 1 in complex with compound 04.
Palte RL
ACS Med Chem Lett
(2021)
[PMID: 34795856 ]
Source organism: Homo sapiens
Assembly composition: protein only structure
Assembly name:
Arginase-1
(Preferred)
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PDBe complex ID:
PDB-CPX-138411 (Preferred)
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Human Arginase 1 in complex with compound 06.
Palte RL
ACS Med Chem Lett
(2021)
[PMID: 34795856 ]
Source organism: Homo sapiens
Assembly composition: protein only structure
Assembly name:
Arginase-1
(Preferred)
search this complex
PDBe complex ID:
PDB-CPX-138411 (Preferred)
search this ID

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