› 4osy

X-ray diffraction
1.91Å resolution

STRUCTURE of FULLY-CLEAVED GLYCINE-BOUND HUMAN L-ASPARAGINASE PROTEIN

Released:
DOI: 10.2210/pdb4osy/pdb
PDB entry 4osy coloured by chain, front view.
PDB entry 4osy coloured by chain, side view.
PDB entry 4osy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Free glycine accelerates the autoproteolytic activation of human asparaginase.
Su Y, Karamitros CS, Nomme J, McSorley T, Konrad M, Lavie A
Chem Biol 20 533-40 (2013)
PMID: 23601642

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
UniProt:
  • Canonical: Q7L266 (Residues: 1-308; Coverage: 100%)
Gene names: ALP, ASRGL1, CRASH
Sequence domains: Asparaginase

Ligands and Environments

2 bound ligands:
Ligand NA 2 x NA
Ligand GLY 4 x GLY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P65
Unit cell:
a: 59.736Å b: 59.736Å c: 301.527Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.182 0.224
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

1 mention without citation

The effects of nature-inspired amino acid substitutions on structural and biochemical properties of the E. coli L-asparaginase EcAIII.
Janicki et al. (2023)