2TOH
TYROSINE HYDROXYLASE CATALYTIC AND TETRAMERIZATION DOMAINS FROM RAT
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE A 501 |
| Chain | Residue |
| A | HOH602 |
| A | HIS331 |
| A | HIS336 |
| A | GLU376 |
| A | HBI500 |
| A | HOH601 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 510 |
| Chain | Residue |
| A | ASN439 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE HBI A 500 |
| Chain | Residue |
| A | LEU294 |
| A | LEU295 |
| A | MTY300 |
| A | GLN310 |
| A | PRO327 |
| A | GLU332 |
| A | TYR371 |
| A | GLU376 |
| A | FE501 |
| A | HOH603 |
| site_id | FE |
| Number of Residues | 3 |
| Details | IRON BINDING SITE. |
| Chain | Residue |
| A | HIS331 |
| A | HIS336 |
| A | GLU376 |
| site_id | MTY |
| Number of Residues | 1 |
| Details | PTERIN BINDING SITE AND SELF-HYDROXYLATED RESIDUE |
| Chain | Residue |
| A | MTY300 |
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 | PRO327-PRO338 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9228951","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9753429","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TOH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2TOH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for substrate specificity","evidences":[{"source":"PubMed","id":"10933781","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P24529","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 14640675, 10747809 |
| Chain | Residue | Details |
| A | SER395 | |
| A | HIS331 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 134 |
| Chain | Residue | Details |
| A | GLY335 | electrostatic stabiliser, hydrogen bond donor, metal ligand |
| A | LEU340 | metal ligand |
| A | CYS380 | metal ligand |
| A | GLU399 | electrostatic stabiliser, hydrogen bond acceptor, steric role |
