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6PAH

HUMAN PHENYLALANINE HYDROXYLASE CATALYTIC DOMAIN DIMER WITH BOUND L-DOPA (3,4-DIHYDROXYPHENYLALANINE) INHIBITOR

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 425
ChainResidue
AHOH649
AHIS285
AHIS290
AGLU330
ADAH600

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DAH A 600
ChainResidue
ALYS199
ALEU248
AHIS285
AHIS290
ATYR325
AGLU330
AFE425
AHOH649

site_idNUL
Number of Residues5
DetailsIRON BINDING LIGANDS
ChainResidue
AHIS285
AHIS290
AGLU330
AHOH649
ADAH600

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 Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P04176
ChainResidueDetails
AHIS285
AHIS290
AGLU330

226707

PDB entries from 2024-10-30

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