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4JPX

Crystal structure of phenylalanine hydroxylase S203P mutant from Chromobacterium violaceum

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 301
ChainResidue
AALA158
AHOH557
ATYR159
ALYS165
ATHR254
AALA255
APRO256
AASP257
APHE258
AHOH418

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 302
ChainResidue
AHIS138
AHIS143
AGLU184
AHOH404
AHOH585

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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