Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1A4U

ALCOHOL DEHYDROGENASE FROM DROSOPHILA LEBANONENSIS

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_idACA
Number of Residues3
DetailsACTIVE SITE, CATALYTIC TRIAD.
ChainResidue
ASER138
ATYR151
ALYS155

site_idACB
Number of Residues3
DetailsACTIVE SITE, CATALYTIC TRIAD.
ChainResidue
BLYS155
BSER138
BTYR151

site_idNAD
Number of Residues1
DetailsNAD/NADP SELECTIVITY AMINO ACID.
ChainResidue
AASP37

site_idND'
Number of Residues1
DetailsNAD/NADP SELECTIVITY AMINO ACID.
ChainResidue
BASP37

site_idNDA
Number of Residues3
DetailsNAD BINDING MOTIF.
ChainResidue
AALA13
AGLY15
AGLY18

site_idNDB
Number of Residues3
DetailsNAD BINDING MOTIF.
ChainResidue
BALA13
BGLY15
BGLY18

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

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ALYS155
ASER138
ATYR151

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BLYS155
BSER138
BTYR151

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ALYS155
AASN107
ASER138
ATYR151

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BLYS155
BASN107
BSER138
BTYR151

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ALYS155
AVAL148

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BLYS155
BVAL148

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ALYS155
ATYR151

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BLYS155
BTYR151

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon