› 1zcf

X-ray diffraction
3Å resolution

L-asparaginase from Erwinia carotovora

Released:
DOI: 10.2210/pdb1zcf/pdb
PDB entry 1zcf coloured by chain, front view.
PDB entry 1zcf coloured by chain, side view.
PDB entry 1zcf coloured by chain, top view.
Source organism: Pectobacterium atrosepticum SCRI1043
Primary publication:
The crystal structure of L-asparaginase from Erwinia carotovora
Kislizin YA, Kravchenko OV, Nikonov SV, Kuranova IP
Kristallografiya 51 (2006)

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 tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180241 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-asparaginase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 327 amino acids
Theoretical weight: 34.53 KDa
Source organism: Pectobacterium atrosepticum SCRI1043
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6Q4F4 (Residues: 20-346; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT GX-6
Spacegroup: P212121
Unit cell:
a: 76.643Å b: 141.992Å c: 260.391Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.203 0.282
Expression system: Escherichia coli BL21(DE3)

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Citations

2 mentions without citation

Tailoring structure-function properties of L-asparaginase: engineering resistance to trypsin cleavage.
Kotzia et al. (2007)
1 more