3KBO
2.14 Angstrom Crystal Structure of Putative Oxidoreductase (ycdW) from Salmonella typhimurium in Complex with NADP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008465 | molecular_function | glycerate dehydrogenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016618 | molecular_function | hydroxypyruvate reductase activity |
| A | 0030267 | molecular_function | glyoxylate reductase (NADPH) activity |
| A | 0051287 | molecular_function | NAD binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008465 | molecular_function | glycerate dehydrogenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016618 | molecular_function | hydroxypyruvate reductase activity |
| B | 0030267 | molecular_function | glyoxylate reductase (NADPH) activity |
| B | 0051287 | molecular_function | NAD binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0008465 | molecular_function | glycerate dehydrogenase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016618 | molecular_function | hydroxypyruvate reductase activity |
| C | 0030267 | molecular_function | glyoxylate reductase (NADPH) activity |
| C | 0051287 | molecular_function | NAD binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0008465 | molecular_function | glycerate dehydrogenase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016618 | molecular_function | hydroxypyruvate reductase activity |
| D | 0030267 | molecular_function | glyoxylate reductase (NADPH) activity |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NDP A 313 |
| Chain | Residue |
| A | ARG89 |
| A | ARG167 |
| A | SER168 |
| A | LYS170 |
| A | LEU197 |
| A | LEU198 |
| A | PRO199 |
| A | LEU225 |
| A | ALA226 |
| A | ARG227 |
| A | ASP251 |
| A | MSE99 |
| A | VAL252 |
| A | HIS275 |
| A | ALA278 |
| A | ARG310 |
| A | TYR312 |
| A | CL315 |
| A | HOH317 |
| A | HOH333 |
| A | HOH336 |
| A | HOH344 |
| A | GLY143 |
| A | HOH358 |
| A | HOH375 |
| A | HOH387 |
| A | HOH446 |
| A | HOH467 |
| A | HOH539 |
| A | ALA144 |
| A | GLY145 |
| A | VAL146 |
| A | LEU147 |
| A | TRP165 |
| A | SER166 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NDB A 314 |
| Chain | Residue |
| A | ASN36 |
| A | PRO38 |
| A | GLU50 |
| A | MSE51 |
| A | ALA53 |
| A | ARG55 |
| A | ARG56 |
| A | HOH323 |
| A | HOH343 |
| A | HOH499 |
| A | HOH546 |
| C | ASN36 |
| C | GLU50 |
| C | ALA53 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 315 |
| Chain | Residue |
| A | TRP45 |
| A | GLY66 |
| A | ARG227 |
| A | NDP313 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 316 |
| Chain | Residue |
| A | ASN11 |
| A | HOH369 |
| site_id | AC5 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NDP B 313 |
| Chain | Residue |
| B | ARG89 |
| B | MSE99 |
| B | GLY143 |
| B | ALA144 |
| B | GLY145 |
| B | VAL146 |
| B | LEU147 |
| B | TRP165 |
| B | SER166 |
| B | ARG167 |
| B | SER168 |
| B | LYS170 |
| B | LEU197 |
| B | LEU198 |
| B | PRO199 |
| B | THR204 |
| B | LEU225 |
| B | ALA226 |
| B | ARG227 |
| B | ASP251 |
| B | VAL252 |
| B | HIS275 |
| B | ALA277 |
| B | ALA278 |
| B | TYR312 |
| B | CL315 |
| B | HOH324 |
| B | HOH333 |
| B | HOH380 |
| B | HOH395 |
| B | HOH430 |
| B | HOH438 |
| B | HOH488 |
| B | HOH489 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EPE B 314 |
| Chain | Residue |
| B | GLN100 |
| B | SER154 |
| B | TRP158 |
| B | HOH547 |
| B | HOH554 |
| C | GLN100 |
| C | ALA157 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 315 |
| Chain | Residue |
| B | NDP313 |
| B | HOH375 |
| B | TRP45 |
| B | GLY66 |
| B | ARG227 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 316 |
| Chain | Residue |
| B | PHE10 |
| B | ASN11 |
| B | TRP15 |
| B | HOH542 |
| site_id | AC9 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NDP C 313 |
| Chain | Residue |
| C | ARG89 |
| C | MSE99 |
| C | GLY143 |
| C | ALA144 |
| C | GLY145 |
| C | VAL146 |
| C | LEU147 |
| C | TRP165 |
| C | SER166 |
| C | ARG167 |
| C | SER168 |
| C | LYS170 |
| C | LEU197 |
| C | LEU198 |
| C | PRO199 |
| C | LEU225 |
| C | ALA226 |
| C | ARG227 |
| C | ASP251 |
| C | HIS275 |
| C | ALA277 |
| C | ALA278 |
| C | TYR312 |
| C | HOH326 |
| C | HOH330 |
| C | HOH371 |
| C | HOH375 |
| C | HOH395 |
| C | HOH421 |
| C | HOH443 |
| C | HOH448 |
| C | HOH454 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 314 |
| Chain | Residue |
| A | ARG56 |
| C | ARG56 |
| C | HOH379 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 315 |
| Chain | Residue |
| C | ASN11 |
| C | TRP15 |
| C | HOH323 |
| site_id | BC3 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NDP D 313 |
| Chain | Residue |
| D | ALA65 |
| D | ARG89 |
| D | MSE99 |
| D | GLY143 |
| D | ALA144 |
| D | GLY145 |
| D | VAL146 |
| D | LEU147 |
| D | TRP165 |
| D | SER166 |
| D | ARG167 |
| D | SER168 |
| D | LYS170 |
| D | LEU197 |
| D | LEU198 |
| D | PRO199 |
| D | THR204 |
| D | LEU225 |
| D | ALA226 |
| D | ARG227 |
| D | ASP251 |
| D | VAL252 |
| D | HIS275 |
| D | ALA277 |
| D | ALA278 |
| D | TYR312 |
| D | CL315 |
| D | HOH325 |
| D | HOH334 |
| D | HOH360 |
| D | HOH362 |
| D | HOH386 |
| D | HOH418 |
| D | HOH483 |
| D | HOH508 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EPE D 314 |
| Chain | Residue |
| D | GLN100 |
| D | SER154 |
| D | TRP158 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL D 315 |
| Chain | Residue |
| D | ALA65 |
| D | GLY66 |
| D | NDP313 |
| D | HOH379 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL D 316 |
| Chain | Residue |
| D | PHE10 |
| D | ASN11 |
| D | TRP15 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01666 |
| Chain | Residue | Details |
| A | ARG227 | |
| B | ARG227 | |
| C | ARG227 | |
| D | ARG227 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01666 |
| Chain | Residue | Details |
| A | HIS275 | |
| B | HIS275 | |
| C | HIS275 | |
| D | HIS275 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1psd |
| Chain | Residue | Details |
| A | HIS275 | |
| A | GLU256 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1psd |
| Chain | Residue | Details |
| B | HIS275 | |
| B | GLU256 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1psd |
| Chain | Residue | Details |
| C | HIS275 | |
| C | GLU256 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1psd |
| Chain | Residue | Details |
| D | HIS275 | |
| D | GLU256 |
