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PDBsum entry 2gdz

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protein ligands links
Oxidoreductase PDB id
2gdz
Jmol
Contents
Protein chain
266 a.a. *
Ligands
NAD
Waters ×303
* Residue conservation analysis
PDB id:
2gdz
Name: Oxidoreductase
Title: Crystal structure of 15-hydroxyprostaglandin dehydrogenase t complexed with NAD+
Structure: NAD+-dependent 15-hydroxyprostaglandin dehydrogen chain: a. Fragment: residues (-1)-265. Synonym: 15 hydroxyprostaglandin dehydrogenase type1. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PDB file)
Resolution:
1.65Å     R-factor:   0.177     R-free:   0.212
Authors: E.S.Pilka,K.Guo,K.Kavanagh,F.Von Delft,C.Arrowsmith,J.Weigel A.Edwards,M.Sundstrom,U.Oppermann,Structural Genomics Conso (Sgc)
Key ref: F.H.Niesen et al. (2010). High-affinity inhibitors of human NAD-dependent 15-hydroxyprostaglandin dehydrogenase: mechanisms of inhibition and structure-activity relationships. PLoS One, 5, e13719. PubMed id: 21072165
Date:
17-Mar-06     Release date:   04-Apr-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P15428  (PGDH_HUMAN) -  15-hydroxyprostaglandin dehydrogenase [NAD(+)]
Seq:
Struc:
266 a.a.
266 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 12 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.1.1.1.141  - 15-hydroxyprostaglandin dehydrogenase (NAD(+)).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: (5Z,13E,15S)-11-alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+ = (5Z,13E)-11-alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH
(5Z,13E,15S)-11-alpha,15-dihydroxy-9-oxoprost-5,13-dienoate
+
NAD(+)
Bound ligand (Het Group name = NAD)
corresponds exactly
= (5Z,13E)-11-alpha-hydroxy-9,15-dioxoprost-5,13-dienoate
+ NADH
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   4 terms 
  Biological process     metabolic process   17 terms 
  Biochemical function     catalytic activity     7 terms  

 

 
    Added reference    
 
 
PLoS One 5:e13719 (2010)
PubMed id: 21072165  
 
 
High-affinity inhibitors of human NAD-dependent 15-hydroxyprostaglandin dehydrogenase: mechanisms of inhibition and structure-activity relationships.
F.H.Niesen, L.Schultz, A.Jadhav, C.Bhatia, K.Guo, D.J.Maloney, E.S.Pilka, M.Wang, U.Oppermann, T.D.Heightman, A.Simeonov.
 
  ABSTRACT  
 
No abstract given.