spacer
spacer

PDBsum entry 2okn

Go to PDB code: 
protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
2okn
Jmol
Contents
Protein chain
477 a.a. *
Ligands
_PI ×3
Metals
_MN ×4
Waters ×301
* Residue conservation analysis
PDB id:
2okn
Name: Hydrolase
Title: Crystal strcture of human prolidase
Structure: Xaa-pro dipeptidase. Chain: a, b. Synonym: x-pro dipeptidase, proline dipeptidase, prolidase, imidodipeptidase. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: pepd, prd. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.45Å     R-factor:   0.180     R-free:   0.231
Authors: U.Mueller,F.H.Niesen,Y.Roske,F.Goetz,J.Behlke,K.Buessow,U.He Protein Structure Factory (Psf)
Key ref: U.Mueller et al. Crystal structure of human prolidase: the molecular basis of pd disease.. To be published, .
Date:
17-Jan-07     Release date:   20-Feb-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P12955  (PEPD_HUMAN) -  Xaa-Pro dipeptidase
Seq:
Struc:
493 a.a.
478 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.4.13.9  - Xaa-Pro dipeptidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of Xaa-|-Pro dipeptides; also acts on aminoacyl- hydroxyproline analogs. No action on Pro-|-Pro.
      Cofactor: Manganese
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular vesicular exosome   1 term 
  Biological process     collagen catabolic process   3 terms 
  Biochemical function     hydrolase activity     8 terms