8c0i

X-ray diffraction
1.9Å resolution

Structure of E. coli Class 2 L-asparaginase EcAIII, mutant M200L (acyl-enzyme intermediate)

Released:

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-273659 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 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 subunit beta Chain: BBB
Molecule details ›
Chain: BBB
Length: 143 amino acids
Theoretical weight: 14.41 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P37595 (Residues: 179-321; Coverage: 45%)
Gene names: JW0812, b0828, iaaA, spt, ybiK
Sequence domains: Asparaginase
Isoaspartyl peptidase subunit beta Chain: DDD
Molecule details ›
Chain: DDD
Length: 143 amino acids
Theoretical weight: 14.53 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P37595 (Residues: 179-321; Coverage: 45%)
Gene names: JW0812, b0828, iaaA, spt, ybiK
Sequence domains: Asparaginase

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU PhotonJet-S
Spacegroup: P212121
Unit cell:
a: 49.71Å b: 74.851Å c: 146.595Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.232 0.275
Expression system: Escherichia coli