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3RJ5

Structure of alcohol dehydrogenase from Drosophila lebanonesis T114V mutant complexed with NAD+

Functional Information from GO Data
ChainGOidnamespacecontents
A0004022molecular_functionalcohol dehydrogenase (NAD+) activity
A0005737cellular_componentcytoplasm
A0006066biological_processalcohol metabolic process
A0016491molecular_functionoxidoreductase activity
A0042802molecular_functionidentical protein binding
B0004022molecular_functionalcohol dehydrogenase (NAD+) activity
B0005737cellular_componentcytoplasm
B0006066biological_processalcohol metabolic process
B0016491molecular_functionoxidoreductase activity
B0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY A 632
ChainResidue
ASER138
ATHR140
ATYR151
AILE183
ANAD850

site_idAC2
Number of Residues29
DetailsBINDING SITE FOR RESIDUE NAD A 850
ChainResidue
AASP37
ATYR62
AASP63
AVAL64
AGLY91
AALA92
AGLY93
AILE106
AILE136
ACYS137
ASER138
ATYR151
ALYS155
APRO181
AGLY182
AILE183
ATHR184
ATHR186
ALEU188
AHOH271
AHOH299
AHOH366
AHOH405
AHOH559
AACY632
AALA12
AGLY15
AGLY16
AILE17

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
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues46
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10366509","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"2707261","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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