3BXX
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 |
| A | 0009718 | biological_process | anthocyanin-containing compound biosynthetic process |
| A | 0009813 | biological_process | flavonoid biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0045552 | molecular_function | dihydrokaempferol 4-reductase activity |
| A | 0047890 | molecular_function | flavanone 4-reductase activity |
| B | 0009718 | biological_process | anthocyanin-containing compound biosynthetic process |
| B | 0009813 | biological_process | flavonoid biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0045552 | molecular_function | dihydrokaempferol 4-reductase activity |
| B | 0047890 | molecular_function | flavanone 4-reductase activity |
| C | 0009718 | biological_process | anthocyanin-containing compound biosynthetic process |
| C | 0009813 | biological_process | flavonoid biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0045552 | molecular_function | dihydrokaempferol 4-reductase activity |
| C | 0047890 | molecular_function | flavanone 4-reductase activity |
| 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 | dihydrokaempferol 4-reductase activity |
| D | 0047890 | molecular_function | flavanone 4-reductase activity |
| E | 0009718 | biological_process | anthocyanin-containing compound biosynthetic process |
| E | 0009813 | biological_process | flavonoid biosynthetic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0045552 | molecular_function | dihydrokaempferol 4-reductase activity |
| E | 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 | dihydrokaempferol 4-reductase activity |
| F | 0047890 | molecular_function | flavanone 4-reductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NAP A 338 |
| Chain | Residue |
| A | SER14 |
| A | THR86 |
| A | PRO87 |
| A | THR126 |
| A | SER127 |
| A | LYS167 |
| A | PRO190 |
| A | THR191 |
| A | LEU192 |
| A | PRO204 |
| A | SER205 |
| A | GLY15 |
| A | PHE16 |
| A | ILE17 |
| A | ARG37 |
| A | LYS44 |
| A | ASP64 |
| A | LEU65 |
| A | ALA85 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE QUE A 342 |
| Chain | Residue |
| A | SER128 |
| A | GLY130 |
| A | TYR163 |
| A | PHE164 |
| D | ALA218 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAP B 338 |
| Chain | Residue |
| B | SER14 |
| B | GLY15 |
| B | PHE16 |
| B | ILE17 |
| B | ARG37 |
| B | LYS44 |
| B | ASP64 |
| B | LEU65 |
| B | ALA85 |
| B | THR86 |
| B | PRO87 |
| B | THR126 |
| B | SER127 |
| B | LYS167 |
| B | PRO190 |
| B | THR191 |
| B | LEU192 |
| B | SER205 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE QUE B 341 |
| Chain | Residue |
| B | SER128 |
| B | ALA129 |
| B | GLY130 |
| B | ASN133 |
| B | LEU192 |
| B | PRO204 |
| B | SER205 |
| B | THR208 |
| B | ILE222 |
| B | GLN227 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE QUE B 342 |
| Chain | Residue |
| B | SER128 |
| B | GLY130 |
| B | ALA160 |
| B | TYR163 |
| B | PHE164 |
| B | PRO204 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NAP C 338 |
| Chain | Residue |
| C | SER14 |
| C | GLY15 |
| C | PHE16 |
| C | ILE17 |
| C | ARG37 |
| C | LYS44 |
| C | ASP64 |
| C | LEU65 |
| C | ALA85 |
| C | THR86 |
| C | THR126 |
| C | SER127 |
| C | SER128 |
| C | LYS167 |
| C | PRO190 |
| C | THR191 |
| C | LEU192 |
| C | PRO204 |
| C | SER205 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE QUE C 341 |
| Chain | Residue |
| C | SER128 |
| C | ALA129 |
| C | ASN133 |
| C | ILE134 |
| C | LEU192 |
| C | PRO204 |
| C | SER205 |
| C | THR208 |
| C | GLN227 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE QUE C 342 |
| Chain | Residue |
| C | SER128 |
| C | GLY130 |
| C | ALA160 |
| C | TYR163 |
| C | PHE164 |
| C | PRO204 |
| site_id | AC9 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NAP D 338 |
| Chain | Residue |
| D | LEU65 |
| D | ALA85 |
| D | THR86 |
| D | PRO87 |
| D | THR126 |
| D | SER127 |
| D | LYS167 |
| D | PRO190 |
| D | THR191 |
| D | LEU192 |
| D | PRO204 |
| D | SER205 |
| D | SER14 |
| D | GLY15 |
| D | PHE16 |
| D | ILE17 |
| D | ARG37 |
| D | LYS44 |
| D | ASP64 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE QUE D 341 |
| Chain | Residue |
| D | SER128 |
| D | ALA129 |
| D | GLY130 |
| D | ASN133 |
| D | LEU192 |
| D | PRO204 |
| D | THR208 |
| D | ILE222 |
| D | GLN227 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE QUE D 342 |
| Chain | Residue |
| A | ALA218 |
| D | MET88 |
| D | SER128 |
| D | GLY130 |
| D | ALA160 |
| D | TYR163 |
| D | PHE164 |
| D | ILE222 |
| site_id | BC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NAP E 338 |
| Chain | Residue |
| E | SER14 |
| E | GLY15 |
| E | PHE16 |
| E | ILE17 |
| E | ARG37 |
| E | LYS44 |
| E | ASP64 |
| E | LEU65 |
| E | ALA85 |
| E | THR86 |
| E | PRO87 |
| E | THR126 |
| E | SER127 |
| E | LYS167 |
| E | PRO190 |
| E | THR191 |
| E | LEU192 |
| E | PRO204 |
| E | SER205 |
| site_id | BC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NAP F 338 |
| Chain | Residue |
| F | SER14 |
| F | GLY15 |
| F | PHE16 |
| F | ILE17 |
| F | ARG37 |
| F | LYS44 |
| F | ASP64 |
| F | LEU65 |
| F | ALA85 |
| F | THR86 |
| F | PRO87 |
| F | THR126 |
| F | SER127 |
| F | LYS167 |
| F | PRO190 |
| F | THR191 |
| F | LEU192 |
| F | PRO204 |
| F | SER205 |
| site_id | BC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE QUE F 341 |
| Chain | Residue |
| F | SER128 |
| F | ALA129 |
| F | GLY130 |
| F | ASN133 |
| F | ILE134 |
| F | LEU192 |
| F | PRO204 |
| F | SER205 |
| F | THR208 |
| F | GLN227 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE QUE F 342 |
| Chain | Residue |
| F | SER128 |
| F | GLY130 |
| F | ALA160 |
| F | TYR163 |
| F | PHE164 |
| F | LYS167 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q12068 |
| Chain | Residue | Details |
| A | LYS167 | |
| B | LYS167 | |
| C | LYS167 | |
| D | LYS167 | |
| E | LYS167 | |
| F | LYS167 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 84 |
| Details | BINDING: BINDING => ECO:0000269|Ref.2, ECO:0007744|PDB:2NNL |
| Chain | Residue | Details |
| A | GLY12 | |
| A | PRO190 | |
| A | PRO204 | |
| A | SER205 | |
| A | THR208 | |
| A | GLN227 | |
| B | GLY12 | |
| B | ARG37 | |
| B | LYS44 | |
| B | ASP64 | |
| B | VAL84 | |
| A | ARG37 | |
| B | SER128 | |
| B | ASN133 | |
| B | TYR163 | |
| B | LYS167 | |
| B | PRO190 | |
| B | PRO204 | |
| B | SER205 | |
| B | THR208 | |
| B | GLN227 | |
| C | GLY12 | |
| A | LYS44 | |
| C | ARG37 | |
| C | LYS44 | |
| C | ASP64 | |
| C | VAL84 | |
| C | SER128 | |
| C | ASN133 | |
| C | TYR163 | |
| C | LYS167 | |
| C | PRO190 | |
| C | PRO204 | |
| A | ASP64 | |
| C | SER205 | |
| C | THR208 | |
| C | GLN227 | |
| D | GLY12 | |
| D | ARG37 | |
| D | LYS44 | |
| D | ASP64 | |
| D | VAL84 | |
| D | SER128 | |
| D | ASN133 | |
| A | VAL84 | |
| D | TYR163 | |
| D | LYS167 | |
| D | PRO190 | |
| D | PRO204 | |
| D | SER205 | |
| D | THR208 | |
| D | GLN227 | |
| E | GLY12 | |
| E | ARG37 | |
| E | LYS44 | |
| A | SER128 | |
| E | ASP64 | |
| E | VAL84 | |
| E | SER128 | |
| E | ASN133 | |
| E | TYR163 | |
| E | LYS167 | |
| E | PRO190 | |
| E | PRO204 | |
| E | SER205 | |
| E | THR208 | |
| A | ASN133 | |
| E | GLN227 | |
| F | GLY12 | |
| F | ARG37 | |
| F | LYS44 | |
| F | ASP64 | |
| F | VAL84 | |
| F | SER128 | |
| F | ASN133 | |
| F | TYR163 | |
| F | LYS167 | |
| A | TYR163 | |
| F | PRO190 | |
| F | PRO204 | |
| F | SER205 | |
| F | THR208 | |
| F | GLN227 | |
| A | LYS167 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | PHE152 | |
| A | LYS156 | |
| A | SER128 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | LYS167 | |
| D | SER128 | |
| D | TYR163 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| E | LYS167 | |
| E | SER128 | |
| E | TYR163 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| F | LYS167 | |
| F | SER128 | |
| F | TYR163 |
| site_id | CSA13 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | PHE152 | |
| A | LYS156 |
| site_id | CSA14 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | PHE152 | |
| B | LYS156 |
| site_id | CSA15 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | PHE152 | |
| C | LYS156 |
| site_id | CSA16 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | PHE152 | |
| D | LYS156 |
| site_id | CSA17 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| E | PHE152 | |
| E | LYS156 |
| site_id | CSA18 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| F | PHE152 | |
| F | LYS156 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | PHE152 | |
| B | LYS156 | |
| B | SER128 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | PHE152 | |
| C | LYS156 | |
| C | SER128 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | PHE152 | |
| D | LYS156 | |
| D | SER128 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| E | PHE152 | |
| E | LYS156 | |
| E | SER128 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| F | PHE152 | |
| F | LYS156 | |
| F | SER128 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS167 | |
| A | SER128 | |
| A | TYR163 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS167 | |
| B | SER128 | |
| B | TYR163 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | LYS167 | |
| C | SER128 | |
| C | TYR163 |
