› 2v3y

X-ray diffraction
1.6Å resolution

His361Ala Escherichia coli aminopeptidase P in complex with product

Released:
DOI: 10.2210/pdb2v3y/pdb
PDB entry 2v3y coloured by chain, front view.
PDB entry 2v3y coloured by chain, side view.
PDB entry 2v3y coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Complexes of mutants of Escherichia coli aminopeptidase P and the tripeptide substrate ValProLeu.
Graham SC, Guss JM
Arch Biochem Biophys 469 200-8 (2008)
PMID: 17983589

Function and Biology Details

Reaction catalysed: 
Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147186 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Xaa-Pro aminopeptidase Chain: A
Molecule details ›
Chain: A
Length: 440 amino acids
Theoretical weight: 49.69 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P15034 (Residues: 2-441; Coverage: 100%)
Gene names: JW2876, b2908, pepP
Sequence domains:
Structure domains:
TRIPEPTIDE (VALINE-PROLINE-LEUCINE) Chain: B
Molecule details ›
Chain: B
Length: 3 amino acids
Theoretical weight: 327 Da
Source organism: Escherichia coli
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand MN 2 x MN
Ligand CL 1 x CL
1 modified residue:
Ligand CSO 1 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200H
Spacegroup: P6422
Unit cell:
a: 177.132Å b: 177.132Å c: 96.17Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.154 0.154 0.167
Expression systems:
  • Escherichia coli
  • Not provided

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Citations

1 review citation

Metallo-aminopeptidase inhibitors.
Mucha et al. (2010)
7 other articles