› 7owj

X-ray diffraction
2.5Å resolution

Odinarchaeota Adenylate kinase (OdinAK) in complex with GTP

Released:
DOI: 10.2210/pdb7owj/pdb
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Source organism: Candidatus Odinarchaeota archaeon LCB_4
Primary publication:
Insights into the evolution of enzymatic specificity and catalysis: From Asgard archaea to human adenylate kinases.
Verma A, Åberg-Zingmark E, Sparrman T, Mushtaq AU, Rogne P, Grundström C, Berntsson R, Sauer UH, Backman L, Nam K, Sauer-Eriksson E, Wolf-Watz M
OpenAccess logo Sci Adv 8 eabm4089 (2022)
PMID: 36332013

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-245391 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenylate kinase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 198 amino acids
Theoretical weight: 22.88 KDa
Source organism: Candidatus Odinarchaeota archaeon LCB_4
Expression system: Escherichia coli

Ligands and Environments

1 bound ligand:
Ligand GTP 6 x GTP
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: MAX IV BEAMLINE BioMAX
Spacegroup: P212121
Unit cell:
a: 77.608Å b: 78.787Å c: 217.191Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.187 0.258
Expression system: Escherichia coli

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Citations

2 citation in other articles

Insights into Enzymatic Catalysis from Binding and Hydrolysis of Diadenosine Tetraphosphate by E. coli Adenylate Kinase.
Tischlik et al. (2023)
1 more

1 mention without citation

Insights into the evolution of enzymatic specificity and catalysis: From Asgard archaea to human adenylate kinases.
Verma et al. (2022)

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