› 1wls

X-ray diffraction
2.16Å resolution

Crystal structure of L-asparaginase I homologue protein from Pyrococcus horikoshii

Released:
DOI: 10.2210/pdb1wls/pdb
PDB entry 1wls coloured by chain, front view.
PDB entry 1wls coloured by chain, side view.
PDB entry 1wls coloured by chain, top view.
Source organism: Pyrococcus horikoshii
Primary publication:
Structure of the type I L-asparaginase from the hyperthermophilic archaeon Pyrococcus horikoshii at 2.16 angstroms resolution.
Yao M, Yasutake Y, Morita H, Tanaka I
Acta Crystallogr D Biol Crystallogr 61 294-301 (2005)
PMID: 15735339

Function and Biology Details

Reaction catalysed: 
L-asparagine + H(2)O = L-aspartate + NH(3)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129611 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
asparaginase Chains: A, B
Molecule details ›
Chains: A, B
Length: 328 amino acids
Theoretical weight: 36.84 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
UniProt:
  • Canonical: O57797 (Residues: 1-328; Coverage: 100%)
Gene name: PH0066
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 24 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P21212
Unit cell:
a: 125.676Å b: 77.2Å c: 98.691Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.211 0.253
Expression system: Escherichia coli

Quick links

Citations

5 review citations

L-asparaginase: a promising chemotherapeutic agent.
Verma et al. (2007)
4 more

3 mentions without citation

Crystal structure and allosteric regulation of the cytoplasmic Escherichia coli L-asparaginase I.
Yun et al. (2007)
2 more