› 1qtr

X-ray diffraction
2.32Å resolution

CRYSTAL STRUCTURE ANALYSIS OF THE PROLYL AMINOPEPTIDASE FROM SERRATIA MARCESCENS

Released:
DOI: 10.2210/pdb1qtr/pdb
PDB entry 1qtr coloured by chain, front view.
PDB entry 1qtr coloured by chain, side view.
PDB entry 1qtr coloured by chain, top view.
Source organism: Serratia marcescens
Primary publication:
Crystal structure of prolyl aminopeptidase from Serratia marcescens.
Yoshimoto T, Kabashima T, Uchikawa K, Inoue T, Tanaka N, Nakamura KT, Tsuru M, Ito K
J Biochem 126 559-65 (1999)
PMID: 10467172

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128448 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Proline iminopeptidase Chain: A
Molecule details ›
Chain: A
Length: 317 amino acids
Theoretical weight: 36.13 KDa
Source organism: Serratia marcescens
Expression system: Escherichia coli
UniProt:
  • Canonical: O32449 (Residues: 1-317; Coverage: 100%)
Gene name: pip
Sequence domains: alpha/beta hydrolase fold
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 RU200
Spacegroup: P43212
Unit cell:
a: 65.36Å b: 65.36Å c: 169.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 0.267
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Bacterial protease inhibitors.
Supuran et al. (2002)
2 more

8 mentions without citation

Bioinformatics perspective on rhomboid intramembrane protease evolution and function.
Kinch et al. (2013)
7 more