1SQI
Structural basis for inhibitor selectivity revealed by crystal structures of plant and mammalian 4-hydroxyphenylpyruvate dioxygenases
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000139 | cellular_component | Golgi membrane |
| A | 0003868 | molecular_function | 4-hydroxyphenylpyruvate dioxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0006559 | biological_process | L-phenylalanine catabolic process |
| A | 0006572 | biological_process | tyrosine catabolic process |
| A | 0009072 | biological_process | aromatic amino acid metabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016701 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051213 | molecular_function | dioxygenase activity |
| B | 0000139 | cellular_component | Golgi membrane |
| B | 0003868 | molecular_function | 4-hydroxyphenylpyruvate dioxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0005794 | cellular_component | Golgi apparatus |
| B | 0006559 | biological_process | L-phenylalanine catabolic process |
| B | 0006572 | biological_process | tyrosine catabolic process |
| B | 0009072 | biological_process | aromatic amino acid metabolic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016701 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE A 1450 |
| Chain | Residue |
| A | HIS183 |
| A | HIS266 |
| A | GLU349 |
| A | 8691501 |
| A | HOH1552 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE A 1451 |
| Chain | Residue |
| A | HOH1712 |
| B | ASP315 |
| A | HIS280 |
| A | HOH1654 |
| A | HOH1655 |
| A | HOH1710 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE B 1452 |
| Chain | Residue |
| B | HIS183 |
| B | HIS266 |
| B | GLU349 |
| B | 8691502 |
| B | HOH1531 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE B 1453 |
| Chain | Residue |
| A | ASP315 |
| B | ARG279 |
| B | HIS280 |
| B | HOH1541 |
| B | HOH1648 |
| B | HOH1659 |
| B | HOH1660 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 869 A 1501 |
| Chain | Residue |
| A | HIS183 |
| A | SER226 |
| A | PRO239 |
| A | ASN241 |
| A | GLN251 |
| A | HIS266 |
| A | PHE336 |
| A | PHE347 |
| A | GLU349 |
| A | PHE359 |
| A | ASN363 |
| A | PHE364 |
| A | FE1450 |
| A | HOH1552 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 869 B 1502 |
| Chain | Residue |
| B | HIS183 |
| B | SER226 |
| B | PRO239 |
| B | ASN241 |
| B | GLN251 |
| B | HIS266 |
| B | LEU289 |
| B | PHE336 |
| B | GLU349 |
| B | PHE359 |
| B | ASN363 |
| B | PHE364 |
| B | FE1452 |
| B | HOH1531 |
| B | HOH1737 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15301540, ECO:0007744|PDB:1SQI |
| Chain | Residue | Details |
| A | HIS183 | |
| A | HIS266 | |
| A | GLU349 | |
| B | HIS183 | |
| B | HIS266 | |
| B | GLU349 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylthreonine => ECO:0000269|PubMed:12867153 |
| Chain | Residue | Details |
| A | THR2 | |
| B | THR2 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P49429 |
| Chain | Residue | Details |
| A | LYS132 | |
| B | LYS132 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P32754 |
| Chain | Residue | Details |
| A | SER211 | |
| B | SER211 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P49429 |
| Chain | Residue | Details |
| A | SER226 | |
| B | SER226 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
| Chain | Residue | Details |
| A | SER250 | |
| B | SER250 |
