› 4o0e

X-ray diffraction
1.71Å resolution

Crystal structure of the human L-asparaginase protein T186V mutant

Released:
DOI: 10.2210/pdb4o0e/pdb
PDB entry 4o0e coloured by chain, front view.
PDB entry 4o0e coloured by chain, side view.
PDB entry 4o0e coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Elucidation of the specific function of the conserved threonine triad responsible for human L-asparaginase autocleavage and substrate hydrolysis.
Nomme J, Su Y, Lavie A
J Mol Biol 426 2471-85 (2014)
PMID: 24768817

Function and Biology Details

Reactions catalysed: 
Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.
L-asparagine + H(2)O = L-aspartate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181624 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isoaspartyl peptidase/L-asparaginase Chains: A, B
Molecule details ›
Chains: A, B
Length: 309 amino acids
Theoretical weight: 32.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q7L266 (Residues: 1-308; Coverage: 100%)
Gene names: ALP, ASRGL1, CRASH
Sequence domains: Asparaginase

Ligands and Environments

1 bound ligand:
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P65
Unit cell:
a: 59.378Å b: 59.378Å c: 298.322Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.175 0.172 0.225
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

A critical review on properties and applications of microbial l-asparaginases.
Krishnapura et al. (2016)
6 more

1 mention without citation

Elucidation of the specific function of the conserved threonine triad responsible for human L-asparaginase autocleavage and substrate hydrolysis.
Nomme et al. (2014)