2XSN
Crystal Structure of Human Tyrosine Hydroxylase Catalytic Domain
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0009072 | biological_process | aromatic amino acid metabolic process |
| A | 0016714 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0009072 | biological_process | aromatic amino acid metabolic process |
| B | 0016714 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0009072 | biological_process | aromatic amino acid metabolic process |
| C | 0016714 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0009072 | biological_process | aromatic amino acid metabolic process |
| D | 0016714 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1528 |
| Chain | Residue |
| A | HIS361 |
| A | HIS366 |
| A | GLU406 |
| A | HOH2067 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1529 |
| Chain | Residue |
| B | HIS361 |
| B | HIS366 |
| B | GLU406 |
| B | HOH2068 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN C 1536 |
| Chain | Residue |
| C | HIS366 |
| C | GLU406 |
| C | HIS361 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN D 1536 |
| Chain | Residue |
| D | HIS361 |
| D | HIS366 |
| D | GLU406 |
Functional Information from PROSITE/UniProt
| site_id | PS00367 |
| Number of Residues | 12 |
| Details | BH4_AAA_HYDROXYL_1 Biopterin-dependent aromatic amino acid hydroxylases signature. PDccHELLGHVP |
| Chain | Residue | Details |
| A | PRO357-PRO368 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P04177","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for substrate specificity","evidences":[{"source":"UniProtKB","id":"P04177","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P24529","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
