1TOH
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 | HIS331 |
A | HIS336 |
A | GLU376 |
A | HOH601 |
A | HOH602 |
A | HOH772 |
site_id | FE |
Number of Residues | 3 |
Details | IRON BINDING SITE. |
Chain | Residue |
A | HIS331 |
A | HIS336 |
A | GLU376 |
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 | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 134 |
Chain | Residue | Details |
A | HIS331 | electrostatic stabiliser, hydrogen bond donor, metal ligand |
A | HIS336 | metal ligand |
A | GLU376 | metal ligand |
A | SER395 | electrostatic stabiliser, hydrogen bond acceptor, steric role |