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1SBY

Alcohol dehydrogenase from Drosophila lebanonensis complexed with NAD+ and 2,2,2-trifluoroethanol at 1.1 A resolution

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
A0042802molecular_functionidentical protein binding
B0004022molecular_functionalcohol dehydrogenase (NAD+) activity
B0005737cellular_componentcytoplasm
B0006066biological_processalcohol metabolic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues31
DetailsBINDING SITE FOR RESIDUE NAD A 1255
ChainResidue
AALA12
AALA92
AGLY93
AILE106
AILE136
ACYS137
ASER138
ATYR151
ALYS155
APRO181
AGLY182
AGLY15
AILE183
ATHR184
ATHR186
ALEU188
AETF1256
AHOH1294
AHOH1302
AHOH1363
AHOH1403
AHOH1486
AGLY16
AHOH1507
AHOH1568
AILE17
AASP37
ATYR62
AASP63
AVAL64
AGLY91

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ETF A 1256
ChainResidue
ALEU95
ASER138
ATHR140
ATYR151
AILE183
ALEU188
AVAL189
ANAD1255

site_idAC3
Number of Residues30
DetailsBINDING SITE FOR RESIDUE NAD B 2255
ChainResidue
BALA12
BGLY15
BGLY16
BILE17
BASP37
BARG38
BTYR62
BASP63
BVAL64
BGLY91
BALA92
BGLY93
BILE106
BILE136
BCYS137
BSER138
BTYR151
BLYS155
BPRO181
BGLY182
BILE183
BTHR184
BTHR186
BPRO187
BLEU188
BETF2256
BHOH2362
BHOH2389
BHOH2405
BHOH2474

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ETF B 2256
ChainResidue
BLEU95
BSER138
BTHR140
BILE145
BTYR151
BILE183
BLEU188
BVAL189
BNAD2255

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 Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ATYR151
BTYR151

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10366509
ChainResidueDetails
APHE10
BPHE10

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ASER138
BSER138

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|PubMed:2707261
ChainResidueDetails
AMET1
BMET1

219869

PDB entries from 2024-05-15

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