Structure of PDB 1w8d Chain A

Receptor sequence
>1w8dA (length=288) Species: 9606 (Homo sapiens) [Search protein sequence]
NTEALQSKFFSPLQKAMLPPNSFQGKVAFITGGGTGLGKGMTTLLSSLGA
QCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKV
AGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLI
KAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMR
FNVIQPGPIKTLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYAS
WINGAVIKFDGGEEVLISGEFNDLRKVTKEQWDTIEEL
3D structure
PDB1w8d Structure and Reactivity of Human Mitochondrial 2,4-Dienoyl-Coa Reductase: Enzyme-Ligand Interactions in a Distinctive Short-Chain Reductase Active Site
ChainA
Resolution2.2 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) G36 T162 A166 V173 P175 K180
Enzyme Commision number 1.3.1.124: 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing].
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NAP A G66 T69 G70 L71 S90 R91 K92 D117 V118 N144 A145 A146 I195 T196 K214 P242 I243 G32 T35 G36 L37 S56 R57 K58 D83 V84 N110 A111 A112 I161 T162 K180 P208 I209
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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Cellular Component
External links
PDB RCSB:1w8d, PDBe:1w8d, PDBj:1w8d
PDBsum1w8d
PubMed15531764
UniProtQ16698|DECR_HUMAN 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing], mitochondrial (Gene Name=DECR1)

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