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1BDB

CIS-BIPHENYL-2,3-DIHYDRODIOL-2,3-DEHYDROGENASE FROM PSEUDOMONAS SP. LB400

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
A0016628molecular_functionoxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor
A0018509molecular_functioncis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase activity
A0019439biological_processaromatic compound catabolic process
A0050664molecular_functionoxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
Functional Information from PDB Data
site_idAC1
Number of Residues28
DetailsBINDING SITE FOR RESIDUE NAD A 300
ChainResidue
AARG41
AGLY58
AASP59
AVAL60
AASN86
ATYR119
ATHR140
AILE141
ASER142
ATYR155
ALYS159
ASER184
AGLY185
AGLY186
AILE187
ASER189
AASP190
ALEU191
AHOH516
AHOH544
AHOH597
AHOH607
AGLY12
ASER15
AGLY16
ALEU17
AASP36
ALYS37

site_idCAT
Number of Residues3
DetailsTHE CATALYTIC TRIAD IS BUILT BY SER 142 - TYR 155 - LYS 159.
ChainResidue
ASER142
ATYR155
ALYS159

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SnagfypnggGplYTAAKHAIvGLVrELA
ChainResidueDetails
ASER142-ALA170

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ATYR155

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:9655331
ChainResidueDetails
AASP59
ALYS159
ALEU9

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ASER142

218500

PDB entries from 2024-04-17

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