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PDBsum entry 3pqf

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protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
3pqf
Jmol
Contents
Protein chains
314 a.a.
Ligands
NAD ×2
Waters ×217
PDB id:
3pqf
Name: Oxidoreductase
Title: Crystal structure of l-lactate dehydrogenase from bacillus s mutation h171c complexed with NAD+
Structure: L-lactate dehydrogenase. Chain: a, b, c, d. Synonym: l-ldh. Engineered: yes. Mutation: yes
Source: Bacillus subtilis. Organism_taxid: 1423. Gene: ldh, lcte, bsu03050. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.49Å     R-factor:   0.190     R-free:   0.235
Authors: Y.Zhang,R.M.Garavito
Key ref: Y.Zhang and r.m.garavito Crystal structure of l-Lactate dehydrogenase from bac subtilis mutation h171c complexed with NAD+. To be published, .
Date:
26-Nov-10     Release date:   11-Jan-12    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P13714  (LDH_BACSU) -  L-lactate dehydrogenase
Seq:
Struc:
320 a.a.
314 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.1.1.1.27  - L-lactate dehydrogenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: (S)-lactate + NAD+ = pyruvate + NADH
(S)-lactate
+
NAD(+)
Bound ligand (Het Group name = NAD)
corresponds exactly
= pyruvate
+ NADH
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     oxidation-reduction process   3 terms 
  Biochemical function     catalytic activity     4 terms