8c23

X-ray diffraction
1.84Å resolution

Structure of E. coli Class 2 L-asparaginase EcAIII, mutant M200T (monoclinic form M200T#m)

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-153446 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Isoaspartyl peptidase subunit alpha Chains: AAA, CCC, EEE, GGG
Molecule details ›
Chains: AAA, CCC, EEE, GGG
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 Chains: BBB, DDD, FFF, HHH
Molecule details ›
Chains: BBB, DDD, FFF, HHH
Length: 143 amino acids
Theoretical weight: 14.4 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

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Spacegroup: C2
Unit cell:
a: 127.461Å b: 149.649Å c: 105.13Å
α: 90° β: 126.718° γ: 90°
R-values:
R R work R free
0.185 0.185 0.216
Expression system: Escherichia coli