1xrm

X-ray diffraction
2.7Å resolution

Crystal structure of active site F1-mutant E213Q soaked with peptide Ala-Phe

Released:

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-161192 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Proline iminopeptidase Chain: A
Molecule details ›
Chain: A
Length: 293 amino acids
Theoretical weight: 33.53 KDa
Source organism: Thermoplasma acidophilum
Expression system: Escherichia coli
UniProt:
  • Canonical: P96084 (Residues: 1-293; Coverage: 100%)
Gene names: Ta0830, pip
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 56.97Å b: 61.92Å c: 80.42Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.251 0.223 0.282
Expression system: Escherichia coli