Structure of PDB 1b16 Chain B

Receptor sequence
>1b16B (length=254) Species: 7225 (Scaptodrosophila lebanonensis) [Search protein sequence]
MDLTNKNVIFVAALGGIGLDTSRELVKRNLKNFVILDRVENPTALAELKA
INPKVNITFHTYDVTVPVAESKKLLKKIFDQLKTVDILINGAGILDDHQI
ERTIAINFTGLVNTTTAILDFWDKRKGGPGGIIANICSVTGFNAIHQVPV
YSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLVHTFNSWLDVEP
RVAELLLSHPTQTSEQCGQNFVKAIEANKNGAIWKLDLGTLEAIEWTKHW
DSHI
3D structure
PDB1b16 The catalytic reaction and inhibition mechanism of Drosophila alcohol dehydrogenase: observation of an enzyme-bound NAD-ketone adduct at 1.4 A resolution by X-ray crystallography.
ChainB
Resolution1.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N107 S138 Y151 K155
Catalytic site (residue number reindexed from 1) N107 S138 Y151 K155
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 NAQ B A12 G15 G16 I17 D37 R38 D63 V64 G91 A92 G93 I106 I136 S138 Y151 K155 P181 G182 I183 T184 T186 L188 V189 A12 G15 G16 I17 D37 R38 D63 V64 G91 A92 G93 I106 I136 S138 Y151 K155 P181 G182 I183 T184 T186 L188 V189
Gene Ontology
Molecular Function
GO:0004022 alcohol dehydrogenase (NAD+) activity
GO:0016491 oxidoreductase activity
GO:0042802 identical protein binding
Biological Process
GO:0006066 alcohol metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1b16, PDBe:1b16, PDBj:1b16
PDBsum1b16
PubMed10366509
UniProtP10807|ADH_DROLE Alcohol dehydrogenase (Gene Name=Adh)

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