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1MMT

Crystal structure of ternary complex of the catalytic domain of human phenylalanine hydroxylase (Fe(II)) complexed with tetrahydrobiopterin and norleucine

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 FE2 A 1425
ChainResidue
AHIS285
AHIS290
AGLU330
AHOH575
AH4B1426

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 428
ChainResidue
AGLU316
APHE351
AGLY352
AGLN355
AHOH527
AHOH550
AARG252
AMET276
APRO314
AASP315

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE H4B A 1426
ChainResidue
AVAL245
AGLY247
ALEU248
ALEU249
ASER251
APHE254
AHIS264
AGLU286
ATYR325
AGLU330
AHOH575
AFE21425

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NLE A 1427
ChainResidue
AARG270
ATYR277
ATHR278
APRO279
ASER349
ASER350
AHOH434
AHOH438

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

218853

PDB entries from 2024-04-24

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