› 3tkj

X-ray diffraction
2.3Å resolution

Crystal Structure of Human Asparaginase-like Protein 1 Thr168Ala

Released:
DOI: 10.2210/pdb3tkj/pdb
PDB entry 3tkj coloured by chain, front view.
PDB entry 3tkj coloured by chain, side view.
PDB entry 3tkj 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:
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: 319 amino acids
Theoretical weight: 33.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7L266 (Residues: 2-308; Coverage: 100%)
Gene names: ALP, ASRGL1, CRASH
Sequence domains: Asparaginase

Ligands and Environments

3 bound ligands:
Ligand NA 2 x NA
Ligand TAM 2 x TAM
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: C2221
Unit cell:
a: 111.682Å b: 111.371Å c: 119.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.168 0.193
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)
13 other articles

2 mentions without citation

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