› 1f2p

X-ray diffraction
1.8Å resolution

CRYSTAL STRUCTURE OF THE STREPTOMYCES GRISEUS AMINOPEPTIDASE COMPLEXED WITH L-PHENYLALANINE

Released:
DOI: 10.2210/pdb1f2p/pdb
PDB entry 1f2p coloured by chain, front view.
PDB entry 1f2p coloured by chain, side view.
PDB entry 1f2p coloured by chain, top view.
Source organism: Streptomyces griseus
Primary publication:
Interactions of Streptomyces griseus aminopeptidase with amino acid reaction products and their implications toward a catalytic mechanism.
Gilboa R, Spungin-Bialik A, Wohlfahrt G, Schomburg D, Blumberg S, Shoham G
Proteins 44 490-504 (2001)
PMID: 11484227

Function and Biology Details

Reaction catalysed: 
Release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160427 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminopeptidase S Chain: A
Molecule details ›
Chain: A
Length: 284 amino acids
Theoretical weight: 29.75 KDa
Source organism: Streptomyces griseus
UniProt:
  • Canonical: P80561 (Residues: 46-329; Coverage: 71%)
Gene name: SGR_5809
Sequence domains: Peptidase family M28
Structure domains: Zn peptidases

Ligands and Environments

3 bound ligands:
Ligand ZN 2 x ZN
Ligand CA 1 x CA
Ligand PHE 1 x PHE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: P41212
Unit cell:
a: 62.18Å b: 62.18Å c: 146.98Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 0.225

Quick links

Citations

21 citation in other articles

Essential roles of zinc ligation and enzyme dimerization for catalysis in the aminoacylase-1/M20 family.
Lindner et al. (2003)
20 more