2Y99
Crystal Structure of cis-Biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)from Pandoraea pnomenusa strain B-356 complex with co-enzyme NAD
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004090 | molecular_function | carbonyl reductase (NADPH) activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016628 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor |
A | 0018509 | molecular_function | cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase activity |
A | 0019439 | biological_process | obsolete aromatic compound catabolic process |
B | 0004090 | molecular_function | carbonyl reductase (NADPH) activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016628 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor |
B | 0018509 | molecular_function | cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase activity |
B | 0019439 | biological_process | obsolete aromatic compound catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE NAD A 1276 |
Chain | Residue |
A | GLY12 |
A | ARG61 |
A | ASN86 |
A | GLY88 |
A | ILE141 |
A | SER142 |
A | TYR155 |
A | LYS159 |
A | PRO184 |
A | MET187 |
A | THR189 |
A | SER15 |
A | ASP190 |
A | LEU191 |
A | HOH2115 |
A | GLY16 |
A | LEU17 |
A | ASP36 |
A | LYS37 |
A | GLY58 |
A | ASP59 |
A | VAL60 |
site_id | AC2 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAD B 1276 |
Chain | Residue |
B | GLY12 |
B | SER15 |
B | GLY16 |
B | LEU17 |
B | ASP36 |
B | LYS37 |
B | GLY58 |
B | ASP59 |
B | VAL60 |
B | ASN86 |
B | GLY88 |
B | ILE141 |
B | SER142 |
B | TYR155 |
B | LYS159 |
B | PRO184 |
B | MET187 |
B | THR189 |
B | ASP190 |
B | LEU191 |
B | ARG192 |
B | HOH2006 |
B | HOH2098 |
Functional Information from PROSITE/UniProt
site_id | PS00061 |
Number of Residues | 29 |
Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SnagfypnggGplYTATKHAVvGLVrQMA |
Chain | Residue | Details |
A | SER142-ALA170 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001 |
Chain | Residue | Details |
A | TYR155 | |
B | TYR155 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ILE10 | |
A | SER142 | |
B | ILE10 | |
B | SER142 |