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Receptor Information

>1e3i Chain B (length=373) Species: 10090 (Mus musculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

GKVIKCKAAIAWKTGSPLCIEEIEVSPPKACEVRIQVIATCVCPTDINAT
DPKKKALFPVVLGHECAGIVESVGPGVTNFKPGDKVIPFFAPQCKRCKLC
LSPLTNLCGKLRNFKYPTIDQELMEDRTSRFTCKGRSIYHFMGVSSFSQY
TVVSEANLARVDDEANLERVCLIGCGFSSGYGAAINTAKVTPGSTCAVFG
LGCVGLSAIIGCKIAGASRIIAIDINGEKFPKAKALGATDCLNPRELDKP
VQDVITELTAGGVDYSLDCAGTAQTLKAAVDCTVLGWGSCTVVGAKVDEM
TIPTVDVILGRSINGTFFGGWKSVDSVPNLVSDYKNKKFDLDLLVTHALP
FESINDAIDLMKEGKSIRTILTF

Ligand ID

NAI

InChI

InChI=1S/C21H29N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1,3-4,7-8,10-11,13-16,20-21,29-32H,2,5-6H2,(H2,23,33)(H,34,35)(H,36,37)(H2,22,24,25)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1

InChIKey

BOPGDPNILDQYTO-NNYOXOHSSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 1.5.0	c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)N5C=CCC(=C5)C(=O)N)O)O)O)O)N
CACTVS 3.341	NC(=O)C1=CN(C=CC1)[C@@H]2O[C@H](CO[P@@](O)(=O)O[P@](O)(=O)OC[C@H]3O[C@H]([C@H](O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0	c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]4[C@H]([C@H]([C@@H](O4)N5C=CCC(=C5)C(=O)N)O)O)O)O)N
CACTVS 3.341	NC(=O)C1=CN(C=CC1)[CH]2O[CH](CO[P](O)(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O

Formula

C21 H29 N7 O14 P2

Name

1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE;
NADH

PDB chain

1e3i Chain B Residue 377 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	1e3i Crystal Structure of Mouse Class II Alcohol Dehydrogenase Reveal Determinants of Substrate Specificity and Catalytic Efficiency
Resolution	2.08 Å
Binding residue (original residue number in PDB)	P47 S182 G203 G205 V207 D227 I228 T278 V296 G297 T319 F320
Binding residue (residue number reindexed from 1)	P44 S179 G200 G202 V204 D224 I225 T275 V293 G294 T316 F317
Annotation score	4

Catalytic site (original residue number in PDB)	C46 P47 T48 N51 H67 E68 C97 C100 C103 C111 R115 C178 S182 R371
Catalytic site (residue number reindexed from 1)	C43 P44 T45 N48 H64 E65 C94 C97 C100 C108 R112 C175 S179 R368
Enzyme Commision number	1.1.1.105: all-trans-retinol dehydrogenase (NAD(+)).

	Molecular Function
GO:0003960	NADPH:quinone reductase activity
GO:0004022	alcohol dehydrogenase (NAD+) activity
GO:0004032	aldose reductase (NADPH) activity
GO:0004745	all-trans-retinol dehydrogenase (NAD+) activity
GO:0005503	all-trans retinal binding
GO:0008270	zinc ion binding
GO:0016491	oxidoreductase activity
GO:0016616	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0018479	benzaldehyde dehydrogenase (NAD+) activity
GO:0019841	retinol binding
GO:0046872	metal ion binding
GO:0051287	NAD binding

	Biological Process
GO:0001523	retinoid metabolic process
GO:0006066	alcohol metabolic process
GO:0006067	ethanol metabolic process
GO:0006081	cellular aldehyde metabolic process
GO:0006629	lipid metabolic process
GO:0010430	fatty acid omega-oxidation
GO:0042572	retinol metabolic process
GO:0044282	small molecule catabolic process
GO:0046164	alcohol catabolic process
GO:1901661	quinone metabolic process

	Cellular Component
GO:0005654	nucleoplasm
GO:0005737	cytoplasm
GO:0005829	cytosol

PDB	RCSB:1e3i, PDBe:1e3i, PDBj:1e3i
PDBsum	1e3i
PubMed	10970744
UniProt	Q9QYY9\|ADH4_MOUSE All-trans-retinol dehydrogenase [NAD(+)] ADH4 (Gene Name=Adh4)

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Structure of PDB 1e3i Chain B Binding Site BS01