2IOD
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAP A 1340 |
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 | MYC1341 |
A | MYC1342 |
A | HOH1343 |
A | HOH1344 |
A | HOH1357 |
A | HOH1366 |
A | HOH1470 |
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 1341 |
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 | NAP1340 |
A | MYC1342 |
A | HOH1348 |
A | HOH1361 |
A | HOH1390 |
A | HOH1470 |
site_id | AC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE MYC A 1342 |
Chain | Residue |
A | SER128 |
A | GLY130 |
A | THR159 |
A | ALA160 |
A | PHE164 |
A | LYS167 |
A | HIS219 |
A | ILE222 |
A | NAP1340 |
A | MYC1341 |
A | HOH1348 |
A | HOH1452 |
A | HOH1462 |
A | HOH1481 |
site_id | AC4 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE NAP B 2340 |
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 | MYC2341 |
B | MYC2342 |
B | HOH2343 |
B | HOH2346 |
B | HOH2349 |
B | HOH2395 |
B | HOH2433 |
B | HOH2511 |
site_id | AC5 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE MYC B 2341 |
Chain | Residue |
B | HOH2360 |
B | HOH2371 |
B | HOH2395 |
B | HOH2399 |
B | SER128 |
B | ALA129 |
B | GLY130 |
B | ASN133 |
B | ILE134 |
B | LEU192 |
B | PRO204 |
B | SER205 |
B | THR208 |
B | GLN227 |
B | NAP2340 |
B | MYC2342 |
site_id | AC6 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE MYC B 2342 |
Chain | Residue |
B | MET88 |
B | SER128 |
B | GLY130 |
B | THR159 |
B | ALA160 |
B | PHE164 |
B | LYS167 |
B | HIS219 |
B | SER221 |
B | ILE222 |
B | NAP2340 |
B | MYC2341 |
B | HOH2366 |
B | HOH2399 |
B | HOH2432 |
B | HOH2437 |
B | HOH2504 |
site_id | AC7 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE NAP C 3340 |
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 | MYC3341 |
C | MYC3342 |
C | HOH3344 |
C | HOH3351 |
C | HOH3354 |
C | HOH3361 |
C | HOH3367 |
C | HOH3439 |
C | HOH3456 |
C | HOH3497 |
site_id | AC8 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE MYC C 3341 |
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 | NAP3340 |
C | MYC3342 |
C | HOH3357 |
C | HOH3360 |
C | HOH3363 |
site_id | AC9 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE MYC C 3342 |
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 | NAP3340 |
C | MYC3341 |
C | HOH3357 |
C | HOH3411 |
C | HOH3429 |
C | HOH3436 |
C | HOH3519 |
site_id | BC1 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE NAP D 4340 |
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 | MYC4341 |
D | MYC4342 |
D | HOH4349 |
D | HOH4356 |
D | HOH4357 |
D | HOH4374 |
D | HOH4375 |
D | HOH4443 |
D | HOH4479 |
D | HOH4496 |
site_id | BC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE MYC D 4341 |
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 | NAP4340 |
D | MYC4342 |
D | HOH4352 |
site_id | BC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE MYC D 4342 |
Chain | Residue |
D | THR86 |
D | MET88 |
D | SER128 |
D | GLY130 |
D | ALA160 |
D | TYR163 |
D | PHE164 |
D | LYS167 |
D | HIS219 |
D | ILE222 |
D | NAP4340 |
D | MYC4341 |
D | HOH4344 |
D | HOH4434 |
D | HOH4451 |
D | HOH4552 |
D | HOH4557 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q12068 |
Chain | Residue | Details |
A | LYS167 | |
B | LYS167 | |
C | LYS167 | |
D | LYS167 |
site_id | SWS_FT_FI2 |
Number of Residues | 56 |
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 | |
A | SER128 | |
A | ASN133 | |
A | TYR163 | |
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 | 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 |