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7ZII

Crystal structure of human tryptophan hydroxylase 1 in complex with inhibitor KM-05-193

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0009072biological_processaromatic amino acid metabolic process
A0016714molecular_functionoxidoreductase 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 PROSITE/UniProt
site_idPS00367
Number of Residues12
DetailsBH4_AAA_HYDROXYL_1 Biopterin-dependent aromatic amino acid hydroxylases signature. PDtcHELLGHVP
ChainResidueDetails
APRO268-PRO279

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P70080
ChainResidueDetails
ATYR235
AARG257
ATHR265
ASER336
AILE366

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:12379098, ECO:0007744|PDB:1MLW
ChainResidueDetails
AHIS272
AHIS277
AGLU317

221051

PDB entries from 2024-06-12

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