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3E2T

The catalytic domain of chicken tryptophan hydroxylase 1 with bound tryptophan

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 Residues3
DetailsBINDING SITE FOR RESIDUE FE A 1
ChainResidue
AHIS273
AHIS278
AGLU318

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 4
ChainResidue
ALYS112
ALYS118
AHOH455

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE IMD A 2
ChainResidue
AGLU318
AHOH473
AHIS273
AGLU274
AHIS278

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE TRP A 3
ChainResidue
ATYR236
AARG258
ATYR265
ATHR266
APRO267
AGLU268
APRO269
AHIS273
AGLU318
APHE319
ASER337
ASER338
AILE367
AHOH416
AHOH422

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGE A 5
ChainResidue
ALEU124
ATYR236
APRO239
AALA310
ACYS365

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PGE A 6
ChainResidue
ATYR126
AGLY127
ASER128
AASP129
ALEU130
AASN140
ALYS144

Functional Information from PROSITE/UniProt
site_idPS00367
Number of Residues12
DetailsBH4_AAA_HYDROXYL_1 Biopterin-dependent aromatic amino acid hydroxylases signature. PDtcHELLGHVP
ChainResidueDetails
APRO269-PRO280

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:18937498
ChainResidueDetails
ATYR236
AARG258
ATHR266
AHIS273
AHIS278
AGLU318
ASER337
AILE367

224572

PDB entries from 2024-09-04

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