Structure of PDB 1w6u Chain C

Receptor sequence
>1w6uC (length=286) Species: 9606 (Homo sapiens) [Search protein sequence]
TEALQSKFFSPLQKAMLPPNSFQGKVAFITGGGTGLGKGMTTLLSSLGAQ
CVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVA
GHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIK
AQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRF
NVIQPGPIKTGAFGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWI
NGAVIKFDGGEEVLISGEFNDLRKVTKEQWDTIEEL
3D structure
PDB1w6u Structure and Reactivity of Human Mitochondrial 2,4-Dienoyl-Coa Reductase: Enzyme-Ligand Interactions in a Distinctive Short-Chain Reductase Active Site
ChainC
Resolution1.75 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G70 T196 A200 V207 P209 K214
Catalytic site (residue number reindexed from 1) G35 T161 A165 V172 P174 K179
Enzyme Commision number 1.3.1.124: 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing].
Interaction with ligand
Gene Ontology
Molecular Function
GO:0008670 2,4-dienoyl-CoA reductase (NADPH) activity
GO:0016491 oxidoreductase activity
GO:0042802 identical protein binding
GO:0070402 NADPH binding
Biological Process
GO:0006631 fatty acid metabolic process
GO:0006635 fatty acid beta-oxidation
GO:0120162 positive regulation of cold-induced thermogenesis
Cellular Component
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix
GO:0005829 cytosol
GO:1902494 catalytic complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1w6u, PDBe:1w6u, PDBj:1w6u
PDBsum1w6u
PubMed15531764
UniProtQ16698|DECR_HUMAN 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing], mitochondrial (Gene Name=DECR1)

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