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3HFB

Crystal structure of human tryoptophan hydroxylase type 1 with LP-534193

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 PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE A 400
ChainResidue
AHIS272
AHIS277
AGLU317
AHOH412
AHOH413
AHOH414

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ML4 A 401
ChainResidue
ATHR265
APRO266
AHIS272
AGLN306
AALA309
APHE313
AGLU317
ASER336
ASER337
ACYS364
AHOH576
AHOH578
AHOH590
AHOH614
AHOH647
AHOH680
APRO238
AARG257
ATYR264

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

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PDB entries from 2024-07-10

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