3C1T
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 | dihydroflavanol 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 | dihydroflavanol 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 | dihydroflavanol 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 | dihydroflavanol 4-reductase activity |
| D | 0047890 | molecular_function | flavanone 4-reductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAP A 340 |
| Chain | Residue |
| A | GLY12 |
| A | VAL84 |
| A | ALA85 |
| A | THR86 |
| A | SER127 |
| A | LYS167 |
| A | PRO190 |
| A | THR191 |
| A | LEU192 |
| A | VAL193 |
| A | PRO204 |
| A | SER14 |
| A | SER205 |
| A | MYC341 |
| A | MYC342 |
| A | HOH343 |
| A | HOH344 |
| A | HOH357 |
| A | HOH366 |
| A | HOH470 |
| A | GLY15 |
| A | PHE16 |
| A | ILE17 |
| A | ARG37 |
| A | LYS44 |
| A | ASP64 |
| A | LEU65 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE MYC A 341 |
| Chain | Residue |
| A | SER128 |
| A | ALA129 |
| A | GLY130 |
| A | ASN133 |
| A | ILE134 |
| A | LEU192 |
| A | PRO204 |
| A | SER205 |
| A | THR208 |
| A | ILE222 |
| A | GLN227 |
| A | NAP340 |
| A | MYC342 |
| A | HOH348 |
| A | HOH361 |
| A | HOH390 |
| A | HOH470 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE MYC A 342 |
| Chain | Residue |
| A | SER128 |
| A | GLY130 |
| A | THR159 |
| A | ALA160 |
| A | PHE164 |
| A | LYS167 |
| A | HIS219 |
| A | ILE222 |
| A | NAP340 |
| A | MYC341 |
| A | HOH348 |
| A | HOH452 |
| A | HOH462 |
| A | HOH481 |
| site_id | AC4 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAP B 340 |
| Chain | Residue |
| B | GLY12 |
| B | SER14 |
| B | GLY15 |
| B | PHE16 |
| B | ILE17 |
| B | ARG37 |
| B | LYS44 |
| B | ASP64 |
| B | LEU65 |
| B | VAL84 |
| B | ALA85 |
| B | THR86 |
| B | PRO87 |
| B | THR126 |
| B | SER127 |
| B | LYS167 |
| B | PRO190 |
| B | THR191 |
| B | LEU192 |
| B | VAL193 |
| B | SER205 |
| B | MYC341 |
| B | MYC342 |
| B | HOH343 |
| B | HOH346 |
| B | HOH349 |
| B | HOH395 |
| B | HOH433 |
| B | HOH511 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE MYC B 341 |
| Chain | Residue |
| B | HOH360 |
| B | HOH371 |
| B | HOH395 |
| B | HOH399 |
| B | SER128 |
| B | ALA129 |
| B | GLY130 |
| B | ASN133 |
| B | ILE134 |
| B | LEU192 |
| B | PRO204 |
| B | SER205 |
| B | THR208 |
| B | GLN227 |
| B | NAP340 |
| B | MYC342 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE MYC B 342 |
| Chain | Residue |
| B | MET88 |
| B | SER128 |
| B | GLY130 |
| B | THR159 |
| B | ALA160 |
| B | PHE164 |
| B | LYS167 |
| B | HIS219 |
| B | SER221 |
| B | ILE222 |
| B | NAP340 |
| B | MYC341 |
| B | HOH366 |
| B | HOH399 |
| B | HOH432 |
| B | HOH437 |
| B | HOH504 |
| site_id | AC7 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAP C 340 |
| Chain | Residue |
| C | SER14 |
| C | GLY15 |
| C | PHE16 |
| C | ILE17 |
| C | ARG37 |
| C | LYS44 |
| C | ASP64 |
| C | LEU65 |
| C | VAL84 |
| C | ALA85 |
| C | THR86 |
| C | PRO87 |
| C | MET88 |
| C | ASP89 |
| C | THR126 |
| C | SER127 |
| C | LYS167 |
| C | PRO190 |
| C | THR191 |
| C | LEU192 |
| C | VAL193 |
| C | SER205 |
| C | MYC341 |
| C | MYC342 |
| C | HOH344 |
| C | HOH351 |
| C | HOH354 |
| C | HOH361 |
| C | HOH367 |
| C | HOH439 |
| C | HOH456 |
| C | HOH497 |
| site_id | AC8 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE MYC C 341 |
| Chain | Residue |
| C | MET88 |
| C | SER128 |
| C | ALA129 |
| C | GLY130 |
| C | ASN133 |
| C | ILE134 |
| C | LEU192 |
| C | PRO204 |
| C | SER205 |
| C | THR208 |
| C | ILE222 |
| C | GLN227 |
| C | NAP340 |
| C | MYC342 |
| C | HOH357 |
| C | HOH360 |
| C | HOH363 |
| site_id | AC9 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE MYC C 342 |
| Chain | Residue |
| B | MET1 |
| B | GLY2 |
| C | MET88 |
| C | SER128 |
| C | GLY130 |
| C | THR159 |
| C | ALA160 |
| C | TYR163 |
| C | PHE164 |
| C | LYS167 |
| C | HIS219 |
| C | ILE222 |
| C | NAP340 |
| C | MYC341 |
| C | HOH357 |
| C | HOH411 |
| C | HOH429 |
| C | HOH436 |
| C | HOH519 |
| site_id | BC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAP D 340 |
| Chain | Residue |
| D | GLY12 |
| D | SER14 |
| D | GLY15 |
| D | PHE16 |
| D | ILE17 |
| D | ARG37 |
| D | LYS44 |
| D | ASP64 |
| D | LEU65 |
| D | VAL84 |
| D | ALA85 |
| D | THR86 |
| D | PRO87 |
| D | MET88 |
| D | THR126 |
| D | SER127 |
| D | LYS167 |
| D | PRO190 |
| D | THR191 |
| D | VAL193 |
| D | SER205 |
| D | MYC341 |
| D | MYC342 |
| D | HOH349 |
| D | HOH356 |
| D | HOH357 |
| D | HOH374 |
| D | HOH375 |
| D | HOH443 |
| D | HOH479 |
| D | HOH496 |
| site_id | BC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE MYC D 341 |
| Chain | Residue |
| D | MET88 |
| D | SER128 |
| D | ALA129 |
| D | GLY130 |
| D | ASN133 |
| D | ILE134 |
| D | LEU192 |
| D | PRO204 |
| D | SER205 |
| D | THR208 |
| D | GLN227 |
| D | NAP340 |
| D | MYC342 |
| D | HOH352 |
| site_id | BC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE MYC D 342 |
| Chain | Residue |
| D | THR86 |
| D | MET88 |
| D | SER128 |
| D | GLY130 |
| D | ALA160 |
| D | TYR163 |
| D | PHE164 |
| D | LYS167 |
| D | HIS219 |
| D | ILE222 |
| D | NAP340 |
| D | MYC341 |
| D | HOH344 |
| D | HOH434 |
| D | HOH451 |
| D | HOH552 |
| D | HOH557 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| 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 | 72 |
| 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 |
| A | PHE152 | |
| A | LYS156 | |
| A | SER128 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | PHE152 | |
| B | LYS156 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | PHE152 | |
| C | LYS156 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | PHE152 | |
| D | 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 |
| A | LYS167 | |
| A | SER128 | |
| A | TYR163 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS167 | |
| B | SER128 | |
| B | TYR163 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | LYS167 | |
| C | SER128 | |
| C | TYR163 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | LYS167 | |
| D | SER128 | |
| D | TYR163 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | PHE152 | |
| A | LYS156 |
