› 2wlt

X-ray diffraction
1.4Å resolution

The crystal structure of Helicobacter pylori L-asparaginase at 1.4 A resolution

Released:
DOI: 10.2210/pdb2wlt/pdb
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Source organism: Helicobacter pylori
Primary publication:
Structure of Helicobacter pylori L-asparaginase at 1.4 A resolution.
Dhavala P, Papageorgiou AC
Acta Crystallogr D Biol Crystallogr 65 1253-61 (2009)
PMID: 19966411

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-195671 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable L-asparaginase Chain: A
Molecule details ›
Chain: A
Length: 332 amino acids
Theoretical weight: 35.61 KDa
Source organism: Helicobacter pylori
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9ZLB9 (Residues: 1-332; Coverage: 100%)
Gene names: ansA, asn, jhp_0661
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ASP 1 x ASP
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: I222
Unit cell:
a: 63.559Å b: 94.796Å c: 100.342Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.126 not available 0.169
Expression system: Escherichia coli

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Citations

3 review citations

Asparaginase in the treatment of non-ALL hematologic malignancies.
Emadi et al. (2014)
2 more

8 mentions without citation

Structural and biophysical aspects of l-asparaginases: a growing family with amazing diversity.
Loch et al. (2021)
7 more

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