› 4et0

X-ray diffraction
3.3Å resolution

Crystal structure of circularly permuted human asparaginase-like protein 1

Released:
DOI: 10.2210/pdb4et0/pdb
PDB entry 4et0 coloured by chain, front view.
PDB entry 4et0 coloured by chain, side view.
PDB entry 4et0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Uncoupling intramolecular processing and substrate hydrolysis in the N-terminal nucleophile hydrolase hASRGL1 by circular permutation.
Li W, Cantor JR, Yogesha SD, Yang S, Chantranupong L, Liu JQ, Agnello G, Georgiou G, Stone EM, Zhang Y
ACS Chem Biol 7 1840-7 (2012)
PMID: 22891768

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:
  • not assigned
Cellular component:
  • not assigned
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: 327 amino acids
Theoretical weight: 33.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7L266 (Residues: 2-167, 168-308; 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: ALS BEAMLINE 5.0.2
Spacegroup: P6522
Unit cell:
a: 108.638Å b: 108.638Å c: 275.144Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.216 0.214 0.249
Expression system: Escherichia coli

Quick links

Citations

1 review citation

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

1 mention without citation

Uncoupling intramolecular processing and substrate hydrolysis in the N-terminal nucleophile hydrolase hASRGL1 by circular permutation.
Li et al. (2012)