Structure of PDB 1axg Chain B

Receptor sequence
>1axgB (length=374) Species: 9796 (Equus caballus) [Search protein sequence]
STAGKVIKCKAAVLWEEKKPFSIEEVEVAPPKAHEVRIKMVATGICRSDD
HVVSGTLVTPLPVIAGHEAAGIVESIGEGVTTVRPGDKVIPLFTPQCGKC
RVCKHPEGNFCLKNDLSMPRGTMQDGTSRFTCRGKPIHHFLGTSTFSQYT
VVDEISVAKIDAASPLEKVCLIGCGFSTGYGSAVKVAKVTQGSTCAVFGL
GGAGLSVIMGCKAAGAARIIGVDINKDKFAKAKEVGATECVNPQDYKKPI
QEVLTEMSNGGVDFSFEVIGRLDTMVTALSCCQEAYGVSVIVGVPPDSQN
LSMNPMLLLSGRTWKGAIFGGFKSKDSVPKLVADFMAKKFALDPLITHVL
PFEKINEGFDLLRSGESIRTILTF
3D structure
PDB1axg A link between protein structure and enzyme catalyzed hydrogen tunneling.
ChainB
Resolution2.5 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
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 ZN B C46 H67 C46 H67
BS02 ZN B C97 C100 C103 C111 C97 C100 C103 C111
BS03 NAD B R47 S48 H51 C174 T178 G199 G201 G202 A203 D223 I224 I269 V292 G293 V294 I318 R47 S48 H51 C174 T178 G199 G201 G202 A203 D223 I224 I269 V292 G293 V294 I318
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:1axg, PDBe:1axg, PDBj:1axg
PDBsum1axg
PubMed9371755
UniProtP00327|ADH1E_HORSE Alcohol dehydrogenase E chain

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