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1MMK

Crystal structure of ternary complex of the catalytic domain of human phenylalanine hydroxylase ((FeII)) complexed with tetrahydrobiopterin and thienylalanine

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 Residues4
DetailsBINDING SITE FOR RESIDUE FE2 A 1426
ChainResidue
AHIS285
AHIS290
AGLU330
AH4B1427

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 429
ChainResidue
AGLY352
AGLN355
AHOH493
AHOH610
AARG252
AMET276
APRO314
AASP315
APHE351

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE H4B A 1427
ChainResidue
AVAL245
AGLY247
ALEU248
ALEU249
ASER251
APHE254
AHIS264
AGLU286
AHIS290
ATRP326
AGLU330
AHOH433
AFE21426

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TIH A 428
ChainResidue
AARG270
ATYR277
ATHR278
AGLU280
APRO281
AHIS285
AGLU330
AGLY346
ASER349
ASER350
AHOH434

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

224931

PDB entries from 2024-09-11

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