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3HF6

Crystal structure of human tryptophan hydroxylase type 1 with bound LP-521834 and FE

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
AHOH421
AHOH516
AHOH517

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE LX0 A 401
ChainResidue
ATYR264
ATHR265
APRO266
AGLU267
APRO268
AHIS272
APHE313
AGLU317
ASER336
ASER337
AHOH418
AHOH432
AHOH438
AHOH449
AHOH506
AGLY234
ATYR235
AARG257

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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