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PDBsum entry 4a73

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protein Protein-protein interface(s) links
Oxidoreductase PDB id
4a73
Jmol
Contents
Protein chains
310 a.a.
Waters ×171
PDB id:
4a73
Name: Oxidoreductase
Title: Single point mutant of thermus thermophilus lactate dehydrog
Structure: L-lactate dehydrogenase. Chain: a, b, c, d. Synonym: l-ldh. Engineered: yes. Mutation: yes
Source: Thermus thermophilus. Organism_taxid: 300852. Strain: hb8. Expressed in: escherichia coli. Expression_system_taxid: 668369.
Resolution:
3.00Å     R-factor:   0.172     R-free:   0.234
Authors: E.De Mendoza-Barbera,F.M.D.Vellieux
Key ref: J.P.Colletier et al. (2012). Sampling the conformational energy landscape of a hyperthermophilic protein by engineering key substitutions. Mol Biol Evol, 29, 1683-1694. PubMed id: 22319152 DOI: 10.1093/molbev/mss015
Date:
10-Nov-11     Release date:   28-Dec-11    
Supersedes: 2xxe
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q5SJA1  (LDH_THET8) -  L-lactate dehydrogenase
Seq:
Struc:
310 a.a.
310 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(+)
= 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: 10.1093/molbev/mss015 Mol Biol Evol 29:1683-1694 (2012)
PubMed id: 22319152  
 
 
Sampling the conformational energy landscape of a hyperthermophilic protein by engineering key substitutions.
J.P.Colletier, A.Aleksandrov, N.Coquelle, S.Mraihi, E.Mendoza-Barberá, M.Field, D.Madern.
 
  ABSTRACT  
 
No abstract given.