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4ANP

Crystal structure of human phenylalanine hydroxylase in complex with a pharmacological chaperone

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 1426
ChainResidue
AHIS285
AHIS290
AGLU330
A3QI1427
AHOH2136

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 3QI A 1427
ChainResidue
ATYR325
ATRP326
AGLU330
AFE1426
AHOH2136
AHOH2152
AHOH2207
APHE254
APRO279
APRO281
AHIS285

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

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PDB entries from 2024-04-24

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