Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

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
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 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:
ChainResidueDetails
AHIS138
AHIS143
AGLU184

223532

PDB entries from 2024-08-07

PDB statisticsPDBj update infoContact PDBjnumon