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PDBsum entry 3pfd

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protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
3pfd

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
368 a.a. *
Ligands
FDA ×4
Metals
IOD ×109
Waters ×623
* Residue conservation analysis
PDB id:
3pfd
Name: Oxidoreductase
Title: Crystal structure of an acyl-coa dehydrogenase from mycobacterium thermoresistibile bound to reduced flavin adenine dinucleotide solved by combined iodide ion sad mr
Structure: Acyl-coa dehydrogenase. Chain: a, b, c, d. Engineered: yes
Source: Mycobacterium thermoresistibile. Organism_taxid: 1797. Strain: atcc 19527 / nctc 10409. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.10Å     R-factor:   0.171     R-free:   0.207
Authors: Seattle Structural Genomics Center For Infectious Disease (Ssgcid)
Key ref: J.Abendroth et al. (2011). SAD phasing using iodide ions in a high-throughput structural genomics environment. J Struct Funct Genomics, 12, 83-95. PubMed id: 21359836
Date:
28-Oct-10     Release date:   10-Nov-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
G7CNE7  (G7CNE7_MYCT3) -  Acyl-CoA dehydrogenase FadE25 from Mycolicibacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 / 316)
Seq:
Struc:
389 a.a.
368 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.3.99.3  - Transferred entry: 1.3.8.7, 1.3.8.8 and 1.3.8.9.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor
Acyl-CoA
+ acceptor
= 2,3-dehydroacyl-CoA
+ reduced acceptor
      Cofactor: FAD
FAD
Bound ligand (Het Group name = FDA) corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
J Struct Funct Genomics 12:83-95 (2011)
PubMed id: 21359836  
 
 
SAD phasing using iodide ions in a high-throughput structural genomics environment.
J.Abendroth, A.S.Gardberg, J.I.Robinson, J.S.Christensen, B.L.Staker, P.J.Myler, L.J.Stewart, T.E.Edwards.
 
  ABSTRACT  
 
No abstract given.

 

 

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