5Z2L
Crystal structure of BdcA in complex with NADPH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0035438 | molecular_function | cyclic-di-GMP binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0044010 | biological_process | single-species biofilm formation |
| A | 0070402 | molecular_function | NADPH binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0035438 | molecular_function | cyclic-di-GMP binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0044010 | biological_process | single-species biofilm formation |
| B | 0070402 | molecular_function | NADPH binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0035438 | molecular_function | cyclic-di-GMP binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0044010 | biological_process | single-species biofilm formation |
| C | 0070402 | molecular_function | NADPH binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0035438 | molecular_function | cyclic-di-GMP binding |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0044010 | biological_process | single-species biofilm formation |
| D | 0070402 | molecular_function | NADPH binding |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0035438 | molecular_function | cyclic-di-GMP binding |
| E | 0042803 | molecular_function | protein homodimerization activity |
| E | 0044010 | biological_process | single-species biofilm formation |
| E | 0070402 | molecular_function | NADPH binding |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0035438 | molecular_function | cyclic-di-GMP binding |
| F | 0042803 | molecular_function | protein homodimerization activity |
| F | 0044010 | biological_process | single-species biofilm formation |
| F | 0070402 | molecular_function | NADPH binding |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0035438 | molecular_function | cyclic-di-GMP binding |
| G | 0042803 | molecular_function | protein homodimerization activity |
| G | 0044010 | biological_process | single-species biofilm formation |
| G | 0070402 | molecular_function | NADPH binding |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0035438 | molecular_function | cyclic-di-GMP binding |
| H | 0042803 | molecular_function | protein homodimerization activity |
| H | 0044010 | biological_process | single-species biofilm formation |
| H | 0070402 | molecular_function | NADPH binding |
| I | 0016491 | molecular_function | oxidoreductase activity |
| I | 0035438 | molecular_function | cyclic-di-GMP binding |
| I | 0042803 | molecular_function | protein homodimerization activity |
| I | 0044010 | biological_process | single-species biofilm formation |
| I | 0070402 | molecular_function | NADPH binding |
| J | 0016491 | molecular_function | oxidoreductase activity |
| J | 0035438 | molecular_function | cyclic-di-GMP binding |
| J | 0042803 | molecular_function | protein homodimerization activity |
| J | 0044010 | biological_process | single-species biofilm formation |
| J | 0070402 | molecular_function | NADPH binding |
| K | 0016491 | molecular_function | oxidoreductase activity |
| K | 0035438 | molecular_function | cyclic-di-GMP binding |
| K | 0042803 | molecular_function | protein homodimerization activity |
| K | 0044010 | biological_process | single-species biofilm formation |
| K | 0070402 | molecular_function | NADPH binding |
| L | 0016491 | molecular_function | oxidoreductase activity |
| L | 0035438 | molecular_function | cyclic-di-GMP binding |
| L | 0042803 | molecular_function | protein homodimerization activity |
| L | 0044010 | biological_process | single-species biofilm formation |
| L | 0070402 | molecular_function | NADPH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue PG0 A 301 |
| Chain | Residue |
| A | GLY89 |
| A | ALA141 |
| C | HIS240 |
| C | HIS242 |
| site_id | AC2 |
| Number of Residues | 33 |
| Details | binding site for residue NDP A 302 |
| Chain | Residue |
| A | ALA38 |
| A | GLY39 |
| A | SER40 |
| A | THR58 |
| A | ASP59 |
| A | SER60 |
| A | ASN82 |
| A | ALA83 |
| A | GLY84 |
| A | ILE85 |
| A | ILE105 |
| A | ILE130 |
| A | GLY131 |
| A | SER132 |
| A | TYR146 |
| A | LYS150 |
| A | PRO176 |
| A | GLY177 |
| A | PRO178 |
| A | ILE179 |
| A | THR181 |
| A | ALA183 |
| A | ASN184 |
| A | HOH406 |
| A | HOH421 |
| A | HOH446 |
| A | HOH454 |
| A | HOH473 |
| A | SER15 |
| A | ARG16 |
| A | GLY17 |
| A | ILE18 |
| A | TYR37 |
| site_id | AC3 |
| Number of Residues | 35 |
| Details | binding site for residue NDP D 301 |
| Chain | Residue |
| D | SER15 |
| D | ARG16 |
| D | GLY17 |
| D | ILE18 |
| D | TYR37 |
| D | ALA38 |
| D | GLY39 |
| D | SER40 |
| D | THR58 |
| D | ASP59 |
| D | SER60 |
| D | ASN82 |
| D | ALA83 |
| D | GLY84 |
| D | ILE85 |
| D | ILE105 |
| D | ILE130 |
| D | GLY131 |
| D | SER132 |
| D | TYR146 |
| D | LYS150 |
| D | PRO176 |
| D | GLY177 |
| D | PRO178 |
| D | ILE179 |
| D | THR181 |
| D | ALA183 |
| D | ASN184 |
| D | HOH424 |
| D | HOH431 |
| D | HOH432 |
| D | HOH433 |
| D | HOH487 |
| D | HOH509 |
| D | HOH536 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 301 |
| Chain | Residue |
| B | VAL140 |
| B | MET143 |
| B | MET193 |
| B | LEU197 |
| B | PHE235 |
| B | HOH415 |
| B | HOH457 |
| D | HOH500 |
| site_id | AC5 |
| Number of Residues | 34 |
| Details | binding site for residue NDP B 302 |
| Chain | Residue |
| B | LYS150 |
| B | PRO176 |
| B | GLY177 |
| B | PRO178 |
| B | ILE179 |
| B | THR181 |
| B | ALA183 |
| B | ASN184 |
| B | HOH405 |
| B | HOH411 |
| B | HOH424 |
| B | HOH478 |
| B | HOH486 |
| B | HOH514 |
| B | HOH532 |
| B | SER15 |
| B | ARG16 |
| B | GLY17 |
| B | ILE18 |
| B | TYR37 |
| B | ALA38 |
| B | GLY39 |
| B | SER40 |
| B | THR58 |
| B | ASP59 |
| B | SER60 |
| B | ASN82 |
| B | ALA83 |
| B | GLY84 |
| B | ILE105 |
| B | ILE130 |
| B | GLY131 |
| B | SER132 |
| B | TYR146 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue GOL C 301 |
| Chain | Residue |
| C | VAL133 |
| C | ASN134 |
| C | PRO176 |
| C | GLY177 |
| C | ASN184 |
| C | PHE235 |
| C | NDP304 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO C 302 |
| Chain | Residue |
| C | ALA61 |
| C | ASP62 |
| C | LYS104 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 303 |
| Chain | Residue |
| C | ASP62 |
| C | ARG63 |
| C | ASP64 |
| C | HOH401 |
| C | HOH414 |
| site_id | AC9 |
| Number of Residues | 35 |
| Details | binding site for residue NDP C 304 |
| Chain | Residue |
| C | SER15 |
| C | ARG16 |
| C | GLY17 |
| C | ILE18 |
| C | TYR37 |
| C | ALA38 |
| C | GLY39 |
| C | SER40 |
| C | THR58 |
| C | ASP59 |
| C | SER60 |
| C | ASN82 |
| C | ALA83 |
| C | GLY84 |
| C | ILE105 |
| C | ILE130 |
| C | GLY131 |
| C | SER132 |
| C | TYR146 |
| C | LYS150 |
| C | PRO176 |
| C | GLY177 |
| C | PRO178 |
| C | ILE179 |
| C | THR181 |
| C | ALA183 |
| C | ASN184 |
| C | GOL301 |
| C | HOH428 |
| C | HOH431 |
| C | HOH433 |
| C | HOH451 |
| C | HOH483 |
| C | HOH494 |
| C | HOH561 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue GOL E 301 |
| Chain | Residue |
| E | TYR146 |
| E | ALA183 |
| E | NDP303 |
| E | HOH418 |
| site_id | AD2 |
| Number of Residues | 36 |
| Details | binding site for residue NDP E 303 |
| Chain | Residue |
| E | GLY13 |
| E | SER15 |
| E | ARG16 |
| E | GLY17 |
| E | ILE18 |
| E | TYR37 |
| E | ALA38 |
| E | GLY39 |
| E | SER40 |
| E | THR58 |
| E | ASP59 |
| E | SER60 |
| E | ASN82 |
| E | ALA83 |
| E | GLY84 |
| E | ILE85 |
| E | ILE105 |
| E | ILE130 |
| E | GLY131 |
| E | SER132 |
| E | TYR146 |
| E | LYS150 |
| E | PRO176 |
| E | GLY177 |
| E | PRO178 |
| E | ILE179 |
| E | THR181 |
| E | ALA183 |
| E | ASN184 |
| E | GOL301 |
| E | HOH411 |
| E | HOH435 |
| E | HOH439 |
| E | HOH448 |
| E | HOH458 |
| E | HOH511 |
| site_id | AD3 |
| Number of Residues | 36 |
| Details | binding site for residue NDP J 301 |
| Chain | Residue |
| J | GLY13 |
| J | SER15 |
| J | ARG16 |
| J | GLY17 |
| J | ILE18 |
| J | TYR37 |
| J | ALA38 |
| J | GLY39 |
| J | SER40 |
| J | THR58 |
| J | ASP59 |
| J | SER60 |
| J | ASN82 |
| J | ALA83 |
| J | GLY84 |
| J | ILE85 |
| J | ILE105 |
| J | ILE130 |
| J | GLY131 |
| J | SER132 |
| J | TYR146 |
| J | LYS150 |
| J | PRO176 |
| J | GLY177 |
| J | PRO178 |
| J | ILE179 |
| J | THR181 |
| J | ALA183 |
| J | ASN184 |
| J | HOH423 |
| J | HOH424 |
| J | HOH432 |
| J | HOH439 |
| J | HOH441 |
| J | HOH450 |
| J | HOH494 |
| site_id | AD4 |
| Number of Residues | 31 |
| Details | binding site for residue NDP H 301 |
| Chain | Residue |
| H | SER15 |
| H | ARG16 |
| H | GLY17 |
| H | ILE18 |
| H | TYR37 |
| H | ALA38 |
| H | GLY39 |
| H | SER40 |
| H | THR58 |
| H | ASP59 |
| H | SER60 |
| H | ASN82 |
| H | ALA83 |
| H | GLY84 |
| H | ILE85 |
| H | ILE105 |
| H | ILE130 |
| H | GLY131 |
| H | SER132 |
| H | TYR146 |
| H | LYS150 |
| H | PRO176 |
| H | GLY177 |
| H | PRO178 |
| H | ILE179 |
| H | THR181 |
| H | ALA183 |
| H | ASN184 |
| H | HOH403 |
| H | HOH404 |
| H | HOH454 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue PEG K 301 |
| Chain | Residue |
| K | ARG202 |
| K | GLU207 |
| K | GLU208 |
| K | HOH496 |
| L | ARG24 |
| L | GLU50 |
| L | HOH420 |
| site_id | AD6 |
| Number of Residues | 35 |
| Details | binding site for residue NDP K 302 |
| Chain | Residue |
| K | GLY13 |
| K | SER15 |
| K | ARG16 |
| K | GLY17 |
| K | ILE18 |
| K | TYR37 |
| K | ALA38 |
| K | GLY39 |
| K | SER40 |
| K | THR58 |
| K | ASP59 |
| K | SER60 |
| K | ASN82 |
| K | ALA83 |
| K | GLY84 |
| K | ILE105 |
| K | ILE130 |
| K | GLY131 |
| K | SER132 |
| K | TYR146 |
| K | LYS150 |
| K | PRO176 |
| K | GLY177 |
| K | PRO178 |
| K | ILE179 |
| K | THR181 |
| K | ALA183 |
| K | ASN184 |
| K | HOH408 |
| K | HOH416 |
| K | HOH424 |
| K | HOH451 |
| K | HOH453 |
| K | HOH464 |
| K | HOH497 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO I 301 |
| Chain | Residue |
| I | ARG16 |
| I | NDP302 |
| I | HOH412 |
| I | HOH589 |
| site_id | AD8 |
| Number of Residues | 34 |
| Details | binding site for residue NDP I 302 |
| Chain | Residue |
| I | SER15 |
| I | ARG16 |
| I | GLY17 |
| I | ILE18 |
| I | TYR37 |
| I | ALA38 |
| I | GLY39 |
| I | SER40 |
| I | THR58 |
| I | ASP59 |
| I | SER60 |
| I | ASN82 |
| I | ALA83 |
| I | GLY84 |
| I | ILE85 |
| I | ILE105 |
| I | ILE130 |
| I | GLY131 |
| I | SER132 |
| I | TYR146 |
| I | LYS150 |
| I | PRO176 |
| I | GLY177 |
| I | PRO178 |
| I | ILE179 |
| I | THR181 |
| I | ALA183 |
| I | ASN184 |
| I | EDO301 |
| I | HOH412 |
| I | HOH422 |
| I | HOH424 |
| I | HOH433 |
| I | HOH518 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue PG4 F 301 |
| Chain | Residue |
| F | HIS240 |
| H | GLY89 |
| H | ALA141 |
| H | GLY142 |
| H | MET143 |
| site_id | AE1 |
| Number of Residues | 37 |
| Details | binding site for residue NDP F 302 |
| Chain | Residue |
| F | GLY13 |
| F | SER15 |
| F | ARG16 |
| F | GLY17 |
| F | ILE18 |
| F | TYR37 |
| F | ALA38 |
| F | GLY39 |
| F | SER40 |
| F | THR58 |
| F | ASP59 |
| F | SER60 |
| F | ASN82 |
| F | ALA83 |
| F | GLY84 |
| F | ILE85 |
| F | ARG101 |
| F | ILE105 |
| F | ILE130 |
| F | GLY131 |
| F | SER132 |
| F | TYR146 |
| F | LYS150 |
| F | PRO176 |
| F | GLY177 |
| F | PRO178 |
| F | ILE179 |
| F | THR181 |
| F | ALA183 |
| F | ASN184 |
| F | HOH410 |
| F | HOH419 |
| F | HOH437 |
| F | HOH447 |
| F | HOH485 |
| F | HOH487 |
| F | HOH494 |
| site_id | AE2 |
| Number of Residues | 1 |
| Details | binding site for residue EDO G 301 |
| Chain | Residue |
| G | HIS240 |
| site_id | AE3 |
| Number of Residues | 32 |
| Details | binding site for residue NDP G 302 |
| Chain | Residue |
| G | GLY13 |
| G | SER15 |
| G | ARG16 |
| G | GLY17 |
| G | ILE18 |
| G | TYR37 |
| G | ALA38 |
| G | GLY39 |
| G | SER40 |
| G | THR58 |
| G | ASP59 |
| G | SER60 |
| G | ASN82 |
| G | ALA83 |
| G | GLY84 |
| G | ILE105 |
| G | ILE130 |
| G | GLY131 |
| G | SER132 |
| G | TYR146 |
| G | LYS150 |
| G | PRO176 |
| G | GLY177 |
| G | PRO178 |
| G | ILE179 |
| G | THR181 |
| G | ALA183 |
| G | ASN184 |
| G | HOH406 |
| G | HOH407 |
| G | HOH414 |
| G | HOH418 |
| site_id | AE4 |
| Number of Residues | 35 |
| Details | binding site for residue NDP L 301 |
| Chain | Residue |
| L | SER15 |
| L | ARG16 |
| L | GLY17 |
| L | ILE18 |
| L | TYR37 |
| L | ALA38 |
| L | GLY39 |
| L | SER40 |
| L | THR58 |
| L | ASP59 |
| L | SER60 |
| L | ASN82 |
| L | ALA83 |
| L | GLY84 |
| L | ILE85 |
| L | ARG101 |
| L | ILE105 |
| L | ILE130 |
| L | GLY131 |
| L | SER132 |
| L | TYR146 |
| L | LYS150 |
| L | PRO176 |
| L | GLY177 |
| L | PRO178 |
| L | ILE179 |
| L | THR181 |
| L | ALA183 |
| L | ASN184 |
| L | HOH409 |
| L | HOH439 |
| L | HOH449 |
| L | HOH504 |
| L | HOH538 |
| L | HOH540 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. VngdrmpvagMaaYAASKSALqGMArGLA |
| Chain | Residue | Details |
| A | VAL133-ALA161 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001 |
| Chain | Residue | Details |
| A | TYR146 | |
| D | TYR146 | |
| B | TYR146 | |
| C | TYR146 | |
| E | TYR146 | |
| J | TYR146 | |
| H | TYR146 | |
| K | TYR146 | |
| I | TYR146 | |
| F | TYR146 | |
| G | TYR146 | |
| L | TYR146 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| H | LEU10 | |
| H | SER132 | |
| K | LEU10 | |
| K | SER132 | |
| I | LEU10 | |
| I | SER132 | |
| F | LEU10 | |
| F | SER132 | |
| G | LEU10 | |
| G | SER132 | |
| L | LEU10 | |
| L | SER132 | |
| A | LEU10 | |
| A | SER132 | |
| D | LEU10 | |
| D | SER132 | |
| B | LEU10 | |
| B | SER132 | |
| C | LEU10 | |
| C | SER132 | |
| E | LEU10 | |
| E | SER132 | |
| J | LEU10 | |
| J | SER132 |
