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X-ray diffraction
1.7Å resolution

Crystal structure of Erwinia chrysanthemi L-asparaginase complexed with 6-HYDROXY-D-NORLEUCINE

Released:
DOI: 10.2210/pdb1jsl/pdb
PDB entry 1jsl coloured by chain, front view.
PDB entry 1jsl coloured by chain, side view.
PDB entry 1jsl coloured by chain, top view.
Source organism: Dickeya chrysanthemi
Primary publication:
Do bacterial L-asparaginases utilize a catalytic triad Thr-Tyr-Glu?
Aghaiypour K, Wlodawer A, Lubkowski J
Biochim Biophys Acta 1550 117-28 (2001)
PMID: 11755201

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139091 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-asparaginase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 327 amino acids
Theoretical weight: 35.12 KDa
Source organism: Dickeya chrysanthemi
UniProt:
  • Canonical: P06608 (Residues: 22-348; Coverage: 100%)
Gene names: ansB, asn
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand DDO 4 x DDO
Ligand 1PE 1 x 1PE
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 106.15Å b: 90.386Å c: 127.37Å
α: 90° β: 91.38° γ: 90°
R-values:
R R work R free
0.21 0.186 0.212

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Citations

4 review citations

L-Asparaginase as potent anti-leukemic agent and its significance of having reduced glutaminase side activity for better treatment of acute lymphoblastic leukaemia.
Ramya et al. (2012)
3 more