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PDBsum entry 4g6g

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protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
4g6g
Jmol
Contents
Protein chains
470 a.a.
Ligands
TRT ×6
FAD ×2
Metals
_MG ×10
Waters ×464
PDB id:
4g6g
Name: Oxidoreductase
Title: Crystal structure of ndh with trt
Structure: Rotenone-insensitive nadh-ubiquinone oxidoreducta mitochondrial. Chain: a, b. Synonym: internal nadh dehydrogenase. Engineered: yes
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: ndi1, yml120c, ym7056.06c. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.39Å     R-factor:   0.195     R-free:   0.234
Authors: W.Li,Y.Feng,J.Ge,M.Yang
Key ref: Y.Feng et al. (2012). Structural insight into the type-II mitochondrial NADH dehydrogenases. Nature, 491, 478-482. PubMed id: 23086143
Date:
19-Jul-12     Release date:   24-Oct-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P32340  (NDI1_YEAST) -  Rotenone-insensitive NADH-ubiquinone oxidoreductase, mitochondrial
Seq:
Struc:
513 a.a.
470 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.6.5.9  - NADH:ubiquinone reductase (non-electrogenic).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: NADH + ubiquinone = NAD+ + ubiquinol
NADH
+
ubiquinone
Bound ligand (Het Group name = TRT)
matches with 50.00% similarity
= NAD(+)
+ ubiquinol
      Cofactor: FAD
FAD
Bound ligand (Het Group name = FAD) corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   4 terms 
  Biological process     oxidation-reduction process   5 terms 
  Biochemical function     oxidoreductase activity     3 terms  

 

 
    reference    
 
 
Nature 491:478-482 (2012)
PubMed id: 23086143  
 
 
Structural insight into the type-II mitochondrial NADH dehydrogenases.
Y.Feng, W.Li, J.Li, J.Wang, J.Ge, D.Xu, Y.Liu, K.Wu, Q.Zeng, J.W.Wu, C.Tian, B.Zhou, M.Yang.
 
  ABSTRACT  
 
No abstract given.