› 5dne

X-ray diffraction
2.39Å resolution

Crystal structure of the Asn-bound guinea pig L-asparaginase 1 catalytic domain active site mutant K188M

Released:
DOI: 10.2210/pdb5dne/pdb
PDB entry 5dne coloured by chain, front view.
PDB entry 5dne coloured by chain, side view.
PDB entry 5dne coloured by chain, top view.
Source organism: Cavia porcellus
Primary publication:
Experimental Data in Support of a Direct Displacement Mechanism for Type I/II L-Asparaginases.
Schalk AM, Antansijevic A, Caffrey M, Lavie A
J Biol Chem 291 5088-100 (2016)
PMID: 26733195

Function and Biology Details

Reaction catalysed: 
L-asparagine + H(2)O = L-aspartate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124711 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
asparaginase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 588 amino acids
Theoretical weight: 63.39 KDa
Source organism: Cavia porcellus
Expression system: Escherichia coli
UniProt:
  • Canonical: H0W0T5 (Residues: 1-565; Coverage: 100%)
Gene name: ASPG
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ASN 4 x ASN
Ligand EDO 9 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: I222
Unit cell:
a: 123.91Å b: 154.79Å c: 157.31Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.194 0.237
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Microbial L-asparaginase for Application in Acrylamide Mitigation from Food: Current Research Status and Future Perspectives.
Jia et al. (2021)
2 more

2 mentions without citation

Experimental Data in Support of a Direct Displacement Mechanism for Type I/II L-Asparaginases.
Schalk et al. (2016)
1 more