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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_processtyrosine 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
A0019293biological_processtyrosine biosynthetic process, by oxidation of phenylalanine
A0046872molecular_functionmetal ion binding
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:
ChainResidueDetails
AHIS138
AHIS143
AGLU184

219140

PDB entries from 2024-05-01

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