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3TCY

Crystallographic structure of phenylalanine hydroxylase from Chromobacterium violaceum (cPAH) bound to 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 Residues10
DetailsBINDING SITE FOR RESIDUE PHE A 302
ChainResidue
AALA158
AHOH481
ATYR159
ALYS165
ATHR254
AALA255
APRO256
AASP257
APHE258
AHOH317

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 298
ChainResidue
AHIS138
AHIS143
AGLU184
AHOH457
AHOH484

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 299
ChainResidue
AHIS22
AGLU68
AHOH411
AHOH463
AHOH508
AHOH516

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 300
ChainResidue
AASP154
ASER216
AASN218
AHOH474
AHOH487
AHOH494

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 301
ChainResidue
AHIS126
AASP245
AASP267

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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