› 1m35

X-ray diffraction
2.4Å resolution

Aminopeptidase P from Escherichia coli

Released:
DOI: 10.2210/pdb1m35/pdb
PDB entry 1m35 coloured by chain, front view.
PDB entry 1m35 coloured by chain, side view.
PDB entry 1m35 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
An orthorhombic form of Escherichia coli aminopeptidase P at 2.4 A resolution.
Graham SC, Lee M, Freeman HC, Guss JM
Acta Crystallogr D Biol Crystallogr 59 897-902 (2003)
PMID: 12777807

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:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147180 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Xaa-Pro aminopeptidase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 440 amino acids
Theoretical weight: 49.74 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:

Ligands and Environments

1 bound ligand:
Ligand MN 12 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: C2221
Unit cell:
a: 209.047Å b: 313.963Å c: 162.034Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 0.215
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

Catalytic properties of the PepQ prolidase from Escherichia coli.
Park et al. (2004)
7 more

1 mention without citation

Structure-Function Relationship of Aminopeptidase P from Pseudomonas aeruginosa.
Peng et al. (2017)