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5DEN

The First Structure of a Full-Length Mammalian Phenylalanine Hydroxylase Reveals the Architecture of an Auto-inhibited Tetramer

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004497molecular_functionmonooxygenase activity
A0004505molecular_functionphenylalanine 4-monooxygenase activity
A0005506molecular_functioniron ion binding
A0006558biological_processL-phenylalanine metabolic process
A0006559biological_processL-phenylalanine catabolic process
A0006571biological_processL-tyrosine biosynthetic process
A0009072biological_processaromatic amino acid metabolic process
A0016491molecular_functionoxidoreductase activity
A0016597molecular_functionamino acid binding
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
A0018126biological_processprotein hydroxylation
A0019293biological_processL-tyrosine biosynthetic process, by oxidation of phenylalanine
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0004497molecular_functionmonooxygenase activity
B0004505molecular_functionphenylalanine 4-monooxygenase activity
B0005506molecular_functioniron ion binding
B0006558biological_processL-phenylalanine metabolic process
B0006559biological_processL-phenylalanine catabolic process
B0006571biological_processL-tyrosine biosynthetic process
B0009072biological_processaromatic amino acid metabolic process
B0016491molecular_functionoxidoreductase activity
B0016597molecular_functionamino acid binding
B0016714molecular_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
B0018126biological_processprotein hydroxylation
B0019293biological_processL-tyrosine biosynthetic process, by oxidation of phenylalanine
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
C0003824molecular_functioncatalytic activity
C0004497molecular_functionmonooxygenase activity
C0004505molecular_functionphenylalanine 4-monooxygenase activity
C0005506molecular_functioniron ion binding
C0006558biological_processL-phenylalanine metabolic process
C0006559biological_processL-phenylalanine catabolic process
C0006571biological_processL-tyrosine biosynthetic process
C0009072biological_processaromatic amino acid metabolic process
C0016491molecular_functionoxidoreductase activity
C0016597molecular_functionamino acid binding
C0016714molecular_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
C0018126biological_processprotein hydroxylation
C0019293biological_processL-tyrosine biosynthetic process, by oxidation of phenylalanine
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
D0003824molecular_functioncatalytic activity
D0004497molecular_functionmonooxygenase activity
D0004505molecular_functionphenylalanine 4-monooxygenase activity
D0005506molecular_functioniron ion binding
D0006558biological_processL-phenylalanine metabolic process
D0006559biological_processL-phenylalanine catabolic process
D0006571biological_processL-tyrosine biosynthetic process
D0009072biological_processaromatic amino acid metabolic process
D0016491molecular_functionoxidoreductase activity
D0016597molecular_functionamino acid binding
D0016714molecular_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
D0018126biological_processprotein hydroxylation
D0019293biological_processL-tyrosine biosynthetic process, by oxidation of phenylalanine
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue FE A 501
ChainResidue
AHIS285
AHIS290
AGLU330
AHOH601
AHOH602

site_idAC2
Number of Residues6
Detailsbinding site for residue FE B 501
ChainResidue
BHOH601
BHOH602
BHIS285
BHIS290
BTYR325
BGLU330

site_idAC3
Number of Residues5
Detailsbinding site for residue FE C 501
ChainResidue
CHIS285
CHIS290
CGLU330
CHOH601
CHOH602

site_idAC4
Number of Residues5
Detailsbinding site for residue FE D 501
ChainResidue
DHIS285
DHIS290
DGLU330
DHOH601
DHOH602

Functional Information from PROSITE/UniProt
site_idPS00367
Number of Residues12
DetailsBH4_AAA_HYDROXYL_1 Biopterin-dependent aromatic amino acid hydroxylases signature. PDicHELLGHVP
ChainResidueDetails
APRO281-PRO292

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues312
DetailsDomain: {"description":"ACT","evidences":[{"source":"PROSITE-ProRule","id":"PRU01007","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10331871","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PHZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PHM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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