3RKU
Substrate Fingerprint and the Structure of NADP+ Dependent Serine Dehydrogenase from Saccharomyces cerevisiae complexed with NADP+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004090 | molecular_function | carbonyl reductase (NADPH) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0031132 | molecular_function | serine 3-dehydrogenase activity |
| A | 0045149 | biological_process | acetoin metabolic process |
| A | 0052588 | molecular_function | diacetyl reductase ((S)-acetoin forming) activity |
| B | 0004090 | molecular_function | carbonyl reductase (NADPH) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0031132 | molecular_function | serine 3-dehydrogenase activity |
| B | 0045149 | biological_process | acetoin metabolic process |
| B | 0052588 | molecular_function | diacetyl reductase ((S)-acetoin forming) activity |
| C | 0004090 | molecular_function | carbonyl reductase (NADPH) activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0031132 | molecular_function | serine 3-dehydrogenase activity |
| C | 0045149 | biological_process | acetoin metabolic process |
| C | 0052588 | molecular_function | diacetyl reductase ((S)-acetoin forming) activity |
| D | 0004090 | molecular_function | carbonyl reductase (NADPH) activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0031132 | molecular_function | serine 3-dehydrogenase activity |
| D | 0045149 | biological_process | acetoin metabolic process |
| D | 0052588 | molecular_function | diacetyl reductase ((S)-acetoin forming) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAP A 268 |
| Chain | Residue |
| A | GLY20 |
| A | ASP75 |
| A | ILE76 |
| A | ASN102 |
| A | ALA103 |
| A | GLY104 |
| A | LYS105 |
| A | GLY154 |
| A | SER155 |
| A | TYR168 |
| A | LYS172 |
| A | SER22 |
| A | PRO198 |
| A | GLY199 |
| A | VAL201 |
| A | THR203 |
| A | GLU204 |
| A | PHE205 |
| A | HOH274 |
| A | HOH296 |
| A | HOH297 |
| A | HOH303 |
| A | ALA23 |
| A | HOH330 |
| A | HOH331 |
| A | HOH348 |
| A | HOH551 |
| A | HOH555 |
| A | GLY24 |
| A | ILE25 |
| A | ALA47 |
| A | ARG48 |
| A | ARG49 |
| A | LEU74 |
| site_id | AC2 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAP B 268 |
| Chain | Residue |
| B | GLY20 |
| B | SER22 |
| B | ALA23 |
| B | GLY24 |
| B | ILE25 |
| B | ALA47 |
| B | ARG48 |
| B | ARG49 |
| B | LEU74 |
| B | ASP75 |
| B | ILE76 |
| B | ASN102 |
| B | ALA103 |
| B | GLY104 |
| B | LYS105 |
| B | LEU153 |
| B | GLY154 |
| B | SER155 |
| B | TYR168 |
| B | LYS172 |
| B | PRO198 |
| B | GLY199 |
| B | VAL201 |
| B | THR203 |
| B | GLU204 |
| B | PHE205 |
| B | HOH275 |
| B | HOH277 |
| B | HOH290 |
| B | HOH291 |
| B | HOH319 |
| B | HOH334 |
| B | HOH417 |
| B | HOH554 |
| site_id | AC3 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAP C 268 |
| Chain | Residue |
| C | HOH419 |
| C | HOH544 |
| C | GLY20 |
| C | SER22 |
| C | ALA23 |
| C | GLY24 |
| C | ILE25 |
| C | ALA47 |
| C | ARG48 |
| C | ARG49 |
| C | LEU74 |
| C | ASP75 |
| C | ILE76 |
| C | ASN102 |
| C | ALA103 |
| C | GLY104 |
| C | LYS105 |
| C | LEU153 |
| C | GLY154 |
| C | TYR168 |
| C | LYS172 |
| C | PRO198 |
| C | GLY199 |
| C | VAL201 |
| C | THR203 |
| C | GLU204 |
| C | PHE205 |
| C | HOH269 |
| C | HOH274 |
| C | HOH279 |
| C | HOH284 |
| C | HOH296 |
| C | HOH351 |
| site_id | AC4 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAP D 268 |
| Chain | Residue |
| D | GLY20 |
| D | SER22 |
| D | ALA23 |
| D | GLY24 |
| D | ILE25 |
| D | ALA47 |
| D | ARG48 |
| D | ARG49 |
| D | LEU74 |
| D | ASP75 |
| D | ILE76 |
| D | ASN102 |
| D | ALA103 |
| D | GLY104 |
| D | LYS105 |
| D | LEU153 |
| D | GLY154 |
| D | TYR168 |
| D | LYS172 |
| D | PRO198 |
| D | GLY199 |
| D | VAL201 |
| D | THR203 |
| D | GLU204 |
| D | PHE205 |
| D | HOH269 |
| D | HOH271 |
| D | HOH273 |
| D | HOH283 |
| D | HOH285 |
| D | HOH297 |
| D | HOH336 |
| D | HOH375 |
| D | HOH553 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SiagrdayptGsiYCASKFAVgAFTdSLR |
| Chain | Residue | Details |
| A | SER155-ARG183 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:O93868 |
| Chain | Residue | Details |
| A | TYR168 | |
| B | TYR168 | |
| C | TYR168 | |
| D | TYR168 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Lowers pKa of active site Tyr => ECO:0000250|UniProtKB:O93868 |
| Chain | Residue | Details |
| A | LYS172 | |
| B | LYS172 | |
| C | LYS172 | |
| D | LYS172 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:L0E2Z4 |
| Chain | Residue | Details |
| A | ILE18 | |
| A | ASP75 | |
| B | ILE18 | |
| B | ASP75 | |
| C | ILE18 | |
| C | ASP75 | |
| D | ILE18 | |
| D | ASP75 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|Ref.7 |
| Chain | Residue | Details |
| A | ASN102 | |
| D | ASN102 | |
| D | TYR168 | |
| D | LYS172 | |
| A | TYR168 | |
| A | LYS172 | |
| B | ASN102 | |
| B | TYR168 | |
| B | LYS172 | |
| C | ASN102 | |
| C | TYR168 | |
| C | LYS172 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:O93868 |
| Chain | Residue | Details |
| A | VAL201 | |
| B | VAL201 | |
| C | VAL201 | |
| D | VAL201 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| A | SER260 | |
| B | SER260 | |
| C | SER260 | |
| D | SER260 |
