› 7qyx

X-ray diffraction
1.85Å resolution

Structure of E.coli Class 2 L-asparaginase EcAIII, mutant RDM1-24 (R207A, D210S, S211T)

Released:
DOI: 10.2210/pdb7qyx/pdb
Model geometry
Fit model/data
PDB entry 7qyx coloured by chain, front view.
PDB entry 7qyx coloured by chain, side view.
PDB entry 7qyx 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

Reactions catalysed: 
Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.
L-asparagine + H(2)O = L-aspartate + NH(3)
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-104776 (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
Isoaspartyl peptidase Chains: BBB, DDD
Molecule details ›
Chains: BBB, DDD
Length: 143 amino acids
Theoretical weight: 14.33 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A3A6SJA6 (Residues: 179-321; Coverage: 45%)
Gene names: NCTC9044_04106, NCTC9702_03859, iaaA
Sequence domains: Asparaginase

Ligands and Environments

2 bound ligands:
Ligand NA 2 x NA
Ligand CL 3 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: 50.258Å b: 74.141Å c: 147.466Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.198 0.238
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)