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1LRM

Crystal structure of binary complex of the catalytic domain of human phenylalanine hydroxylase with dihydrobiopterin (BH2)

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 Residues7
DetailsBINDING SITE FOR RESIDUE FE A 428
ChainResidue
AHIS285
AHIS290
AGLU330
AHBI429
AHOH1143
AHOH1145
AHOH1174

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HBI A 429
ChainResidue
ALEU249
ASER251
APHE254
ATYR325
AFE428
AHOH1111
AHOH1143
AHOH1145
AHOH1155
AVAL245
AGLY247

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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