› 7qym

X-ray diffraction
1.2Å resolution

Structure of E.coli Class 2 L-asparaginase EcAIII, mutant RDM1-18 (R207V, D210P, S211W)

Released:
DOI: 10.2210/pdb7qym/pdb
Model geometry
Fit model/data
PDB entry 7qym coloured by chain, front view.
PDB entry 7qym coloured by chain, side view.
PDB entry 7qym coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural and biophysical studies of new L-asparaginase variants: lessons from random mutagenesis of the prototypic Escherichia coli Ntn-amidohydrolase.
Loch JI, Klonecka A, Kądziołka K, Bonarek P, Barciszewski J, Imiolczyk B, Brzezinski K, Gilski M, Jaskolski M
OpenAccess logo Acta Crystallogr D Struct Biol 78 911-926 (2022)
PMID: 35775990

Function and Biology Details

Reaction catalysed: 
Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-100350 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Isoaspartyl peptidase subunit alpha Chains: AAA, CCC
Molecule details ›
Chains: AAA, CCC
Length: 178 amino acids
Theoretical weight: 19.01 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P37595 (Residues: 1-178; Coverage: 56%)
Gene names: JW0812, b0828, iaaA, spt, ybiK
Sequence domains: Asparaginase
Beta-aspartyl-peptidase Chains: BBB, DDD
Molecule details ›
Chains: BBB, DDD
Length: 143 amino acids
Theoretical weight: 14.45 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A066T6R7 (Residues: 179-321; Coverage: 45%)
Gene names: EPS76_07410, GRC73_03160, HIE29_000291, OGM49_07615, R8O40_000076, iaaA
Sequence domains: Asparaginase

Ligands and Environments

2 bound ligands:
Ligand NA 2 x NA
Ligand CL 5 x CL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Spacegroup: P212121
Unit cell:
a: 49.552Å b: 75.006Å c: 146.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.127 0.127 0.153
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

The effects of nature-inspired amino acid substitutions on structural and biochemical properties of the E. coli L-asparaginase EcAIII.
Janicki et al. (2023)

1 mention without citation

Structural and biophysical studies of new L-asparaginase variants: lessons from random mutagenesis of the prototypic Escherichia coli Ntn-amidohydrolase.
Loch et al. (2022)