PDBsum entry: 2vig

Oxidoreductase

PDB id: 2vig

Contents

Protein chains

(+ 2 more) 379 a.a. *

Ligands

FAD ×8

EDO ×12

COS ×5

Waters ×1134

* Residue conservation analysis

PDB id:

2vig

Name:

Oxidoreductase

Title:

Crystal structure of human short-chain acyl coa dehydrogenase

Structure:

Short-chain specific acyl-coa dehydrogenase,. Chain: a, b, c, d, e, f, g, h. Fragment: residues 30-412. Synonym: scad, butyryl-coa dehydrogenase, acyl coa dehydrogenase. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: r3-prare2.

Resolution:

1.90Å R-factor: 0.199 R-free: 0.231

Authors:

A.C.W.Pike,N.Pantic,E.Parizotto,O.Gileadi,E.Ugochukwu, F.Von Delft,J.Weigelt,C.H.Arrowsmith,A.Edwards,U.Oppermann

Key ref:

A.C.W.Pike et al. Crystal structure of human short-Chain acyl coa dehydrogenase. To be published,

Date:

30-Nov-07 Release date: 25-Dec-07

Protein chains

P16219  (ACADS_HUMAN) -  Short-chain specific acyl-CoA dehydrogenase, mitochondrial

Seq: 412 a.a.

Struc: 379 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.1.3.8.1 - Butyryl-CoA dehydrogenase.
• Reaction: Butanoyl-CoA + electron-transfer flavoprotein = 2-butenoyl-CoA + reduced electron-transfer flavoprotein

Butanoyl-CoA (Bound ligand (Het Group name = COS) matches with 88.00% similarity) + electron-transfer flavoprotein = 2-butenoyl-CoA + reduced electron-transfer flavoprotein

• 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 

• Cellular component: mitochondrion (2 terms)
• Biological process: metabolic process (11 terms)
• Biochemical function: oxidoreductase activity (6 terms)