4H8N
Crystal structure of conjugated polyketone reductase C2 from candida parapsilosis complexed with NADPH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005575 | cellular_component | cellular_component |
| A | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016652 | molecular_function | oxidoreductase activity, acting on NAD(P)H as acceptor |
| A | 0036441 | molecular_function | 2-dehydropantolactone reductase activity |
| A | 0042180 | biological_process | ketone metabolic process |
| A | 0047011 | molecular_function | 2-dehydropantolactone reductase (A-specific) activity |
| B | 0005575 | cellular_component | cellular_component |
| B | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016652 | molecular_function | oxidoreductase activity, acting on NAD(P)H as acceptor |
| B | 0036441 | molecular_function | 2-dehydropantolactone reductase activity |
| B | 0042180 | biological_process | ketone metabolic process |
| B | 0047011 | molecular_function | 2-dehydropantolactone reductase (A-specific) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NDP A 3001 |
| Chain | Residue |
| A | GLY24 |
| A | ASN162 |
| A | GLN186 |
| A | PHE214 |
| A | SER215 |
| A | PRO216 |
| A | LEU217 |
| A | ALA221 |
| A | ARG222 |
| A | ALA244 |
| A | VAL259 |
| A | THR25 |
| A | THR260 |
| A | THR261 |
| A | SER262 |
| A | SER263 |
| A | LYS264 |
| A | ARG267 |
| A | HOH3114 |
| A | HOH3192 |
| A | HOH3219 |
| B | LYS28 |
| A | GLY26 |
| B | GLU224 |
| A | THR27 |
| A | LYS28 |
| A | ASP58 |
| A | TYR63 |
| A | HIS125 |
| A | SER161 |
| site_id | AC2 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NDP B 3001 |
| Chain | Residue |
| A | LYS28 |
| A | GLU224 |
| B | GLY24 |
| B | THR25 |
| B | GLY26 |
| B | THR27 |
| B | LYS28 |
| B | ASP58 |
| B | TYR63 |
| B | LYS88 |
| B | HIS125 |
| B | SER161 |
| B | ASN162 |
| B | GLN186 |
| B | PHE214 |
| B | SER215 |
| B | PRO216 |
| B | LEU217 |
| B | ALA221 |
| B | ARG222 |
| B | ALA244 |
| B | VAL259 |
| B | THR260 |
| B | THR261 |
| B | SER262 |
| B | SER263 |
| B | LYS264 |
| B | ARG267 |
| B | HOH3113 |
| B | HOH3168 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"23828603","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23828603","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4H8N","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Lowers pKa of active site Tyr","evidences":[{"source":"PubMed","id":"23828603","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
