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1B2L

ALCOHOL DEHYDROGENASE FROM DROSOPHILA LEBANONENSIS: TERNARY COMPLEX WITH NAD-CYCLOHEXANONE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004022molecular_functionalcohol dehydrogenase (NAD+) activity
A0005737cellular_componentcytoplasm
A0006066biological_processalcohol metabolic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0018455molecular_functionalcohol dehydrogenase [NAD(P)+] activity
A0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CA A 301
ChainResidue
AASP2
AASP2
ATHR4
ATHR4
AHOH306
AHOH306
AHOH325
AHOH325

site_idAC2
Number of Residues34
DetailsBINDING SITE FOR RESIDUE NDC A 255
ChainResidue
AALA12
AGLY15
AGLY16
AILE17
AASP37
ATYR62
AASP63
AVAL64
AGLY91
AALA92
AGLY93
ALEU95
AILE106
AILE136
ACYS137
ASER138
ATHR140
AILE145
ATYR151
ALYS155
APRO181
AGLY182
AILE183
ATHR184
ACYH256
ADTT257
AHOH311
AHOH374
AHOH406
AHOH413
AHOH448
AHOH469
AHOH489
AHOH530

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CYH A 256
ChainResidue
AGLY93
AILE94
ALEU95
AHIS190
ANDC255
AHOH402
AHOH530

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DTT A 257
ChainResidue
ATHR184
AHIS190
ANDC255
AHOH358
AHOH412
AHOH530

site_idACA
Number of Residues3
DetailsCATALYTIC TRIAD
ChainResidue
ASER138
ATYR151
ALYS155

site_idCAA
Number of Residues2
DetailsCA2+ BINDING RESIDUES
ChainResidue
AASP2
ATHR4

site_idNA1
Number of Residues3
DetailsNAD BINDING MOTIF IN DADHS G(A)XGXXG
ChainResidue
AALA13
AGLY15
AGLY18

site_idNA2
Number of Residues3
DetailsNAD BINDING MOTIF IN SDRS GXXXGXG
ChainResidue
AALA12
AGLY16
AGLY18

site_idNA3
Number of Residues1
DetailsNAD/NADP SELECTIVITY AMINO ACID
ChainResidue
AASP37

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SvtgfnaihqVpvYSASKAAVvSFTnSLA
ChainResidueDetails
ASER138-ALA166

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ATYR151

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10366509
ChainResidueDetails
APHE10

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ASER138

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|PubMed:2707261
ChainResidueDetails
AMET1

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PDB entries from 2024-04-24

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