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4Q3W

Crystal structure of C. violaceum phenylalanine hydroxylase D139E mutation

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
A0016491molecular_functionoxidoreductase activity
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 Residues5
DetailsBINDING SITE FOR RESIDUE CO A 301
ChainResidue
AHIS138
AHIS143
AGLU184
AHOH401
AHOH402

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 302
ChainResidue
AGLU139
AHOH538
AGLY100
ALEU101
AILE102
ATHR119

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AHIS138
AHIS143
AGLU184

218853

PDB entries from 2024-04-24

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