› 2zch

X-ray diffraction
2.83Å resolution

Crystal structure of human prostate specific antigen complexed with an activating antibody

Released:
DOI: 10.2210/pdb2zch/pdb
PDB entry 2zch coloured by chain, front view.
PDB entry 2zch coloured by chain, side view.
PDB entry 2zch coloured by chain, top view.
Source organisms:
Primary publication:
Crystal structure of a ternary complex between human prostate-specific antigen, its substrate acyl intermediate and an activating antibody.
Ménez R, Michel S, Muller BH, Bossus M, Ducancel F, Jolivet-Reynaud C, Stura EA
J Mol Biol 376 1021-33 (2008)
PMID: 18187150

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: -Tyr-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-233926 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Prostate-specific antigen Chain: P
Molecule details ›
Chain: P
Length: 237 amino acids
Theoretical weight: 26.12 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P07288 (Residues: 25-261; Coverage: 97%)
Gene names: APS, KLK3
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
monoclonal antibody 8G8F5 Fab Chain: L
Molecule details ›
Chain: L
Length: 215 amino acids
Theoretical weight: 23.44 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins
monoclonal antibody 8G8F5 Fab Chain: H
Molecule details ›
Chain: H
Length: 229 amino acids
Theoretical weight: 24.37 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins

Ligands and Environments

3 bound ligands:
Ligand NDG 2 x NDG
Ligand CL 1 x CL
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P41212
Unit cell:
a: 87.36Å b: 87.36Å c: 236.332Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.203 0.27

Quick links

Citations

13 review citations

Functional roles of human kallikrein-related peptidases.
Sotiropoulou et al. (2009)
12 more

11 mentions without citation

Natural and synthetic inhibitors of kallikrein-related peptidases (KLKs).
Goettig et al. (2010)
10 more