X-ray diffraction
2.3Å resolution

Crystal structure of inactive F1-mutant G37A


Function and Biology Details

Reaction catalysed:
Release of N-terminal proline from a peptide.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Proline iminopeptidase Chain: A
Molecule details ›
Chain: A
Length: 293 amino acids
Theoretical weight: 33.54 KDa
Source organism: Thermoplasma acidophilum
Expression system: Escherichia coli
  • Canonical: P96084 (Residues: 1-293; Coverage: 100%)
Gene names: Ta0830, pip
Sequence domains: Serine aminopeptidase, S33
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 55.28Å b: 57.73Å c: 82.7Å
α: 90° β: 90° γ: 90°
R R work R free
0.254 0.242 0.286
Expression system: Escherichia coli