› 4amz

X-ray diffraction
2Å resolution

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN WITH A COVALENTLY BOUND INHIBITOR IC-2

Released:
DOI: 10.2210/pdb4amz/pdb
PDB entry 4amz coloured by chain, front view.
PDB entry 4amz coloured by chain, side view.
PDB entry 4amz coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Molecular dynamics, crystallography and mutagenesis studies on the substrate gating mechanism of prolyl oligopeptidase.
Kaszuba K, Róg T, Danne R, Canning P, Fülöp V, Juhász T, Szeltner Z, St Pierre JF, García-Horsman A, Männistö PT, Karttunen M, Hokkanen J, Bunker A
Biochimie 94 1398-411 (2012)
PMID: 22484394

Function and Biology Details

Reaction catalysed: 
Hydrolysis of --Pro-|- and to a lesser extent --Ala-|- in oligopeptides.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150042 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prolyl endopeptidase Chain: A
Molecule details ›
Chain: A
Length: 710 amino acids
Theoretical weight: 80.86 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli
UniProt:
  • Canonical: P23687 (Residues: 1-710; Coverage: 100%)
Gene name: PREP
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand 2P4 1 x 2P4
Ligand GOL 5 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P212121
Unit cell:
a: 71.1Å b: 99.5Å c: 110.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.159 0.204
Expression system: Escherichia coli

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Citations

6 review citations

Enzyme Tunnels and Gates As Relevant Targets in Drug Design.
Marques et al. (2017)
5 more