Structure of PDB 6o91 Chain B

Receptor sequence
>6o91B (length=374) Species: 9796 (Equus caballus) [Search protein sequence]
STAGKVIKCKAAVLWEEKKPFSIEEVEVAPPKAHEVRIKMVATGICRSDD
HVVSGTFVTPLPVIAGHEAAGIVESIGEGVTTVRPGDKVIPLFTPQCGKC
RVCKHPEGNFCLKNDLSMPRGTMQDGTSRFTCRGKPIHHFLGTSTFSQYT
VVDEISVAKIDAASPLEKVCLIGCGFSTGYGSAVKVAKVTQGSTCAVFGL
GGVGLSVIMGCKAAGAARIIGVDINKDKFAKAKEVGATECVNPQDYKKPI
QEVLTEMSNGGVDFSFEVIGRLDTMVTALSCCQEAYGVSVIVGVPPDSQN
LSMNPMLLLSGRTWKGAIFGGFKSKDSVPKLVADFMAKKFALDPLITHVL
PFEKINEGFDLLRSGESIRTILTF
3D structure
PDB6o91 Substitutions of Amino Acid Residues in the Substrate Binding Site of Horse Liver Alcohol Dehydrogenase Have Small Effects on the Structures but Significantly Affect Catalysis of Hydrogen Transfer.
ChainB
Resolution1.1 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 S48 H51 H67 C174
Catalytic site (residue number reindexed from 1) C46 S48 H51 H67 C174
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:6o91, PDBe:6o91, PDBj:6o91
PDBsum6o91
PubMed31994873
UniProtP00327|ADH1E_HORSE Alcohol dehydrogenase E chain

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