4zm9

X-ray diffraction
2.51Å resolution

Crystal structure of circularly permuted human asparaginase-like protein 1

Released:
Source organism: Homo sapiens

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-181624 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isoaspartyl peptidase/L-asparaginase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 327 amino acids
Theoretical weight: 33.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q7L266 (Residues: 2-167, 168-308; Coverage: 100%)
Gene names: ALP, ASRGL1, CRASH
Sequence domains: Asparaginase

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P212121
Unit cell:
a: 104.308Å b: 111.107Å c: 122.517Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.204 0.233
Expression system: Escherichia coli BL21(DE3)