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3TK2

Crystallographic structure of phenylalanine hydroxylase from Chromobacterium violaceum cocrystallized with phenylalanine in a site distal to the active site

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0004505molecular_functionphenylalanine 4-monooxygenase activity
A0005506molecular_functioniron ion binding
A0006559biological_processL-phenylalanine catabolic process
A0006571biological_processL-tyrosine biosynthetic process
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 Residues11
DetailsBINDING SITE FOR RESIDUE PHE A 298
ChainResidue
AALA158
AHOH452
AHOH478
ATYR159
ALYS165
ALEU178
ATHR254
APRO256
AASP257
APHE258
AHOH370

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 299
ChainResidue
AHIS138
AHIS143
AGLU184
AHOH344
AHOH362

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO A 300
ChainResidue
AHIS22
AGLU68
AHOH333
AHOH334

Functional Information from PROSITE/UniProt
site_idPS00367
Number of Residues12
DetailsBH4_AAA_HYDROXYL_1 Biopterin-dependent aromatic amino acid hydroxylases signature. PDvfHDLFGHVP
ChainResidueDetails
APRO134-PRO145

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBinding site: {}
ChainResidueDetails

253389

PDB entries from 2026-05-13

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