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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
A0004497molecular_functionmonooxygenase activity
A0004505molecular_functionphenylalanine 4-monooxygenase activity
A0005506molecular_functioniron ion binding
A0006558biological_processL-phenylalanine metabolic process
A0006559biological_processL-phenylalanine catabolic process
A0006571biological_processtyrosine biosynthetic process
A0009072biological_processaromatic amino acid metabolic process
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
A0019293biological_processtyrosine biosynthetic process, by oxidation of phenylalanine
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
B0004497molecular_functionmonooxygenase activity
B0004505molecular_functionphenylalanine 4-monooxygenase activity
B0005506molecular_functioniron ion binding
B0006558biological_processL-phenylalanine metabolic process
B0006559biological_processL-phenylalanine catabolic process
B0006571biological_processtyrosine biosynthetic process
B0009072biological_processaromatic amino acid metabolic process
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
B0019293biological_processtyrosine biosynthetic process, by oxidation of phenylalanine
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
C0004497molecular_functionmonooxygenase activity
C0004505molecular_functionphenylalanine 4-monooxygenase activity
C0005506molecular_functioniron ion binding
C0006558biological_processL-phenylalanine metabolic process
C0006559biological_processL-phenylalanine catabolic process
C0006571biological_processtyrosine biosynthetic process
C0009072biological_processaromatic amino acid metabolic process
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
C0019293biological_processtyrosine biosynthetic process, by oxidation of phenylalanine
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
D0004497molecular_functionmonooxygenase activity
D0004505molecular_functionphenylalanine 4-monooxygenase activity
D0005506molecular_functioniron ion binding
D0006558biological_processL-phenylalanine metabolic process
D0006559biological_processL-phenylalanine catabolic process
D0006571biological_processtyrosine biosynthetic process
D0009072biological_processaromatic amino acid metabolic process
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
D0019293biological_processtyrosine 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 Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:10331871, ECO:0007744|PDB:1PHZ, ECO:0007744|PDB:2PHM
ChainResidueDetails
AHIS285
DHIS285
DHIS290
DGLU330
AHIS290
AGLU330
BHIS285
BHIS290
BGLU330
CHIS285
CHIS290
CGLU330

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P16331
ChainResidueDetails
AALA2
BALA2
CALA2
DALA2

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:7387651, ECO:0007744|PubMed:22673903
ChainResidueDetails
ASER16
BSER16
CSER16
DSER16

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PDB entries from 2024-11-06

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