2NNL
Binding of two substrate analogue molecules to dihydroflavonol-4-reductase alters the functional geometry of the catalytic site
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| D | 0009718 | biological_process | anthocyanin-containing compound biosynthetic process |
| D | 0009813 | biological_process | flavonoid biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0045552 | molecular_function | dihydroflavanol 4-reductase activity |
| D | 0047890 | molecular_function | flavanone 4-reductase activity |
| F | 0009718 | biological_process | anthocyanin-containing compound biosynthetic process |
| F | 0009813 | biological_process | flavonoid biosynthetic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0045552 | molecular_function | dihydroflavanol 4-reductase activity |
| F | 0047890 | molecular_function | flavanone 4-reductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAP D 1330 |
| Chain | Residue |
| D | SER14 |
| D | ALA85 |
| D | THR86 |
| D | MET88 |
| D | THR126 |
| D | SER127 |
| D | TYR163 |
| D | LYS167 |
| D | PRO190 |
| D | THR191 |
| D | VAL193 |
| D | GLY15 |
| D | PRO204 |
| D | SER205 |
| D | ERD1331 |
| D | HOH1333 |
| D | HOH1359 |
| D | HOH1369 |
| D | HOH1406 |
| D | HOH1573 |
| D | HOH1574 |
| D | HOH1575 |
| D | PHE16 |
| D | HOH1576 |
| D | HOH1577 |
| D | HOH1578 |
| D | HOH1580 |
| D | ILE17 |
| D | ARG37 |
| D | LYS44 |
| D | ASP64 |
| D | LEU65 |
| D | VAL84 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ERD D 1331 |
| Chain | Residue |
| D | PHE90 |
| D | SER128 |
| D | ASN133 |
| D | ILE134 |
| D | TYR163 |
| D | LEU192 |
| D | PRO204 |
| D | SER205 |
| D | THR208 |
| D | ILE222 |
| D | GLN227 |
| D | NAP1330 |
| D | HOH1494 |
| D | HOH1500 |
| D | HOH1580 |
| D | HOH1581 |
| site_id | AC3 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NAP F 2330 |
| Chain | Residue |
| F | GLY12 |
| F | SER14 |
| F | GLY15 |
| F | PHE16 |
| F | ILE17 |
| F | ARG37 |
| F | LYS44 |
| F | ASP64 |
| F | LEU65 |
| F | VAL84 |
| F | ALA85 |
| F | THR86 |
| F | PRO87 |
| F | MET88 |
| F | THR126 |
| F | SER127 |
| F | TYR163 |
| F | LYS167 |
| F | PRO190 |
| F | THR191 |
| F | LEU192 |
| F | VAL193 |
| F | PRO204 |
| F | SER205 |
| F | ERD2331 |
| F | HOH2338 |
| F | HOH2342 |
| F | HOH2423 |
| F | HOH2631 |
| F | HOH2632 |
| F | HOH2633 |
| F | HOH2634 |
| F | HOH2635 |
| F | HOH2637 |
| F | HOH2639 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ERD F 2331 |
| Chain | Residue |
| F | SER128 |
| F | ASN133 |
| F | ILE134 |
| F | TYR163 |
| F | LEU192 |
| F | PRO204 |
| F | SER205 |
| F | THR208 |
| F | ILE222 |
| F | GLN227 |
| F | NAP2330 |
| F | HOH2530 |
| F | HOH2545 |
| F | HOH2638 |
| F | HOH2639 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q12068","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2006","submissionDatabase":"PDB data bank","title":"Binding of two substrate analogue molecules to dihydroflavonol-4-reductase alters the functional geometry of the catalytic site.","authors":["Petit P.","Langlois D'Estaintot B.","Granier T.","Gallois B."]}},{"source":"PDB","id":"2NNL","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | PHE152 | |
| D | LYS156 | |
| D | SER128 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| F | PHE152 | |
| F | LYS156 | |
| F | SER128 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | LYS167 | |
| D | SER128 | |
| D | TYR163 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| F | LYS167 | |
| F | SER128 | |
| F | TYR163 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | PHE152 | |
| D | LYS156 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| F | PHE152 | |
| F | LYS156 |
