5yhp

X-ray diffraction
2.39Å resolution

Proline iminopeptidase from Psychrophilic yeast glaciozyma antarctica

Released:
Source organism: Glaciozyma antarctica
Entry authors: Rodzli NA, Kamaruddin S, Jonet A, Seman WMKW, Tab MM, Minor N, Jaafar NR, Mahadi NM, Murad AMA, Bakar FDA, Illias RMD

Function and Biology Details

Reaction catalysed:
Release of N-terminal proline from a peptide.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-104230 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Proline iminopeptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 355 amino acids
Theoretical weight: 39.57 KDa
Source organism: Glaciozyma antarctica
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A2H4A311 (Residues: 1-344; Coverage: 100%)
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Unit cell:
a: 55.388Å b: 82.269Å c: 171.005Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.186 0.215
Expression system: Escherichia coli