2OBY
Crystal structure of Human P53 inducible oxidoreductase (TP53I3,PIG3)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003960 | molecular_function | NADPH:quinone reductase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006739 | biological_process | NADP metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0048038 | molecular_function | quinone binding |
| A | 0070402 | molecular_function | NADPH binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003960 | molecular_function | NADPH:quinone reductase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006739 | biological_process | NADP metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0048038 | molecular_function | quinone binding |
| B | 0070402 | molecular_function | NADPH binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0003960 | molecular_function | NADPH:quinone reductase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0006739 | biological_process | NADP metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0048038 | molecular_function | quinone binding |
| C | 0070402 | molecular_function | NADPH binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0003960 | molecular_function | NADPH:quinone reductase activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0006739 | biological_process | NADP metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0048038 | molecular_function | quinone binding |
| D | 0070402 | molecular_function | NADPH binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0003960 | molecular_function | NADPH:quinone reductase activity |
| E | 0005829 | cellular_component | cytosol |
| E | 0006739 | biological_process | NADP metabolic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0042803 | molecular_function | protein homodimerization activity |
| E | 0048038 | molecular_function | quinone binding |
| E | 0070402 | molecular_function | NADPH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAP A 1400 |
| Chain | Residue |
| A | ASN40 |
| A | GLY173 |
| A | LYS177 |
| A | TYR192 |
| A | ILE217 |
| A | TYR221 |
| A | TYR238 |
| A | GLY239 |
| A | MET241 |
| A | GLY242 |
| A | SER264 |
| A | ARG41 |
| A | LEU265 |
| A | LEU266 |
| A | MET317 |
| A | ASN320 |
| A | ASN322 |
| A | GLU123 |
| A | THR127 |
| A | ALA148 |
| A | SER151 |
| A | GLY152 |
| A | VAL153 |
| A | ALA172 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NAP B 1401 |
| Chain | Residue |
| B | ASN40 |
| B | ARG41 |
| B | GLU123 |
| B | THR127 |
| B | ALA148 |
| B | SER151 |
| B | GLY152 |
| B | VAL153 |
| B | ALA172 |
| B | GLY173 |
| B | LYS177 |
| B | TYR192 |
| B | ILE217 |
| B | TYR238 |
| B | MET241 |
| B | SER264 |
| B | LEU265 |
| B | LEU266 |
| B | MET317 |
| B | ASN322 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NAP C 1402 |
| Chain | Residue |
| C | ARG41 |
| C | GLU123 |
| C | THR127 |
| C | ALA148 |
| C | SER151 |
| C | GLY152 |
| C | VAL153 |
| C | ALA172 |
| C | GLY173 |
| C | LYS177 |
| C | TYR192 |
| C | ILE217 |
| C | TYR221 |
| C | TYR238 |
| C | MET241 |
| C | SER264 |
| C | LEU266 |
| C | MET317 |
| C | ASN322 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAP D 1403 |
| Chain | Residue |
| D | ASN40 |
| D | ARG41 |
| D | GLU123 |
| D | THR127 |
| D | ALA148 |
| D | SER151 |
| D | GLY152 |
| D | VAL153 |
| D | ALA172 |
| D | GLY173 |
| D | LYS177 |
| D | TYR192 |
| D | TYR221 |
| D | TYR238 |
| D | MET241 |
| D | SER264 |
| D | LEU265 |
| D | LEU266 |
| D | MET317 |
| D | ASN320 |
| D | ASN322 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAP E 1404 |
| Chain | Residue |
| E | MET241 |
| E | SER264 |
| E | LEU265 |
| E | LEU266 |
| E | MET317 |
| E | ASN320 |
| E | ASN322 |
| E | ASN40 |
| E | ARG41 |
| E | GLU123 |
| E | THR127 |
| E | ALA148 |
| E | SER151 |
| E | GLY152 |
| E | VAL153 |
| E | ALA172 |
| E | GLY173 |
| E | LYS177 |
| E | TYR192 |
| E | ILE217 |
| E | TYR221 |
| E | TYR238 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 30 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19349281 |
| Chain | Residue | Details |
| A | ARG41 | |
| B | TYR192 | |
| B | SER264 | |
| B | ASN322 | |
| C | ARG41 | |
| C | ALA148 | |
| C | GLY173 | |
| C | TYR192 | |
| C | SER264 | |
| C | ASN322 | |
| D | ARG41 | |
| A | ALA148 | |
| D | ALA148 | |
| D | GLY173 | |
| D | TYR192 | |
| D | SER264 | |
| D | ASN322 | |
| E | ARG41 | |
| E | ALA148 | |
| E | GLY173 | |
| E | TYR192 | |
| E | SER264 | |
| A | GLY173 | |
| E | ASN322 | |
| A | TYR192 | |
| A | SER264 | |
| A | ASN322 | |
| B | ARG41 | |
| B | ALA148 | |
| B | GLY173 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | MOD_RES: N-acetylmethionine => ECO:0000269|Ref.9 |
| Chain | Residue | Details |
| A | MET1 | |
| B | MET1 | |
| C | MET1 | |
| D | MET1 | |
| E | MET1 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1guf |
| Chain | Residue | Details |
| A | TYR51 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1guf |
| Chain | Residue | Details |
| B | TYR51 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1guf |
| Chain | Residue | Details |
| C | TYR51 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1guf |
| Chain | Residue | Details |
| D | TYR51 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1guf |
| Chain | Residue | Details |
| E | TYR51 |
