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2PAH

TETRAMERIC HUMAN PHENYLALANINE HYDROXYLASE

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
B0004497molecular_functionmonooxygenase activity
B0004505molecular_functionphenylalanine 4-monooxygenase activity
B0005506molecular_functioniron ion binding
B0006559biological_processL-phenylalanine catabolic process
B0009072biological_processaromatic amino acid metabolic process
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
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FE A 453
ChainResidue
AHIS285
AHIS290
AGLU330

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FE B 454
ChainResidue
BHIS285
BHIS290
BGLU330

site_idFE1
Number of Residues3
Details
ChainResidue
AHIS285
AHIS290
AGLU330

site_idFE2
Number of Residues3
Details
ChainResidue
BHIS285
BHIS290
BGLU330

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 Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P04176","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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