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PDBsum entry 3vph

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protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
3vph
Jmol
Contents
Protein chains
310 a.a.
Ligands
OXM ×4
FBP ×2
NAD ×3
GOL ×4
Waters ×448
PDB id:
3vph
Name: Oxidoreductase
Title: L-lactate dehydrogenase from thermus caldophilus gk24 comple oxamate, nadh and fbp
Structure: L-lactate dehydrogenase. Chain: a, b, c, d. Synonym: l-ldh. Engineered: yes
Source: Thermus caldophilus. Organism_taxid: 272. Gene: ldh. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.00Å     R-factor:   0.209     R-free:   0.246
Authors: K.Arai,T.Ohno,A.Miyanaga,S.Fushinobu,H.Taguchi
Key ref: Y.Ikehara et al. (2014). The Core of Allosteric Motion in Thermus caldophilus l-Lactate Dehydrogenase. J Biol Chem, 289, 31550-31564. PubMed id: 25258319 DOI: 10.1074/jbc.M114.599092
Date:
01-Mar-12     Release date:   06-Mar-13    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P06150  (LDH_THECA) -  L-lactate dehydrogenase
Seq:
Struc:
310 a.a.
310 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 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
Bound ligand (Het Group name = OXM)
matches with 71.43% similarity
+
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   4 terms 
  Biochemical function     catalytic activity     4 terms  

 

 
    reference    
 
 
DOI no: 10.1074/jbc.M114.599092 J Biol Chem 289:31550-31564 (2014)
PubMed id: 25258319  
 
 
The Core of Allosteric Motion in Thermus caldophilus l-Lactate Dehydrogenase.
Y.Ikehara, K.Arai, N.Furukawa, T.Ohno, T.Miyake, S.Fushinobu, M.Nakajima, A.Miyanaga, H.Taguchi.
 
  ABSTRACT  
 
No abstract given.