Structure of PDB 3oq6 Chain B

Receptor sequence
>3oq6B (length=374) Species: 9796 (Equus caballus) [Search protein sequence]
STAGKVIKCKAAVLWEEKKPFSIEEVEVAPPKAHEVRIKMVATGICRSDD
HVVSGTLVTPLPVIAGHEAAGIVESIGEGVTTVRPGDKVIPLFTPQCGKC
RVCKHPEGNFCLKNDLSMPRGTMQDGTSRFTCRGKPIHHFLGTSTFSQYT
VVDEISVAKIDAASPLEKVCLIGCGFSTGYGSAVKVAKVTQGSTCAVFGL
GGVGLSVIMGCKAAGAARIIGVDINKDKFAKAKEVGATECVNPQDYKKPI
QEVLTEMSNGGVDFSFEVIGRLDTMVTALSCCQEAYGVSVIVGVPPDSQN
LSMNPMLLLSGRTWKGCIFGGFKSKDSVPKLVADFMAKKFALDPLITHVL
PFEKINEGFDLLRSGESIRTILTF
3D structure
PDB3oq6 Origins of the high catalytic activity of human alcohol dehydrogenase 4 studied with horse liver A317C alcohol dehydrogenase.
ChainB
Resolution1.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C46 R47 S48 H51 H67 E68 C97 C100 C103 C111 D115 C174 T178 R369
Catalytic site (residue number reindexed from 1) C46 R47 S48 H51 H67 E68 C97 C100 C103 C111 D115 C174 T178 R369
Enzyme Commision number 1.1.1.1: alcohol dehydrogenase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004022 alcohol dehydrogenase (NAD+) activity
GO:0004745 all-trans-retinol dehydrogenase (NAD+) activity
GO:0008270 zinc ion binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
Biological Process
GO:0042572 retinol metabolic process
GO:0042573 retinoic acid metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3oq6, PDBe:3oq6, PDBj:3oq6
PDBsum3oq6
PubMed21184752
UniProtP00327|ADH1E_HORSE Alcohol dehydrogenase E chain

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