› 1igb

X-ray diffraction
2.3Å resolution

AEROMONAS PROTEOLYTICA AMINOPEPTIDASE COMPLEXED WITH THE INHIBITOR PARA-IODO-D-PHENYLALANINE HYDROXAMATE

Released:
DOI: 10.2210/pdb1igb/pdb
PDB entry 1igb coloured by chain, front view.
PDB entry 1igb coloured by chain, side view.
PDB entry 1igb coloured by chain, top view.
Source organism: Vibrio proteolyticus
Primary publication:
The structure of the Aeromonas proteolytica aminopeptidase complexed with a hydroxamate inhibitor. Involvement in catalysis of Glu151 and two zinc ions of the co-catalytic unit.
Chevrier B, D'Orchymont H, Schalk C, Tarnus C, Moras D
Eur J Biochem 237 393-8 (1996)
PMID: 8647077

Function and Biology Details

Reaction catalysed: 
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169610 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bacterial leucyl aminopeptidase Chain: A
Molecule details ›
Chain: A
Length: 291 amino acids
Theoretical weight: 31.43 KDa
Source organism: Vibrio proteolyticus
UniProt:
  • Canonical: Q01693 (Residues: 107-397; Coverage: 60%)
Sequence domains: Peptidase family M28
Structure domains: Zn peptidases

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand IPO 1 x IPO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: P6122
Unit cell:
a: 109.15Å b: 109.15Å c: 98.35Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.16 0.16 0.241

Quick links

Citations

2 review citations

Zinc enzymes.
Coleman JE. (1998)
1 more

2 mentions without citation

Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation.
Huang et al. (2005)
1 more