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PDBe Entry: 1tg2 view

Crystal structure of phenylalanine hydroxylase A313T mutant with 7,8-dihydrobiopterin bound
Summary
Header OXIDOREDUCTASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.2 Å, R-factor: 21.3%, Free R-factor: 25.4%, Spacegroup: C 2 2 21
Released 30/11/2004, deposition: 28/05/2004, last revision: 24/02/2009
Authors Erlandsen, H.search; Pey, A.L.search; Gamez, A.search; Perez, B.search; Desviat, L.R.search; Aguado, C.search; Koch, R.search; Surendran, S.search; Tyring, S.search; Matalon, R.search; Scriver, C.R.search; Ugarte, M.search; Martinez, A.search; Stevens, R.C.search
Primary citation Correction of kinetic and stability defects by tetrahydrobiopterin in phenylketonuria patients with certain phenylalanine hydroxylase mutations.
PROC.NATL.ACAD.SCI.USAsearch vol:101, pag:16903-16908 (2004) [PubMed ID 15557004 ]search
Keywords phenylalanine hydroxylase phenylketonuria mutant A313T in complex with cofactor analogue 7search, 8-dihydrobiopterinsearch, OXIDOREDUCTASEsearch
EC 1.14.16.1 ExPASy BRENDA search (A)
Organism Homo sapiens(human) 9606search(A)
UniProt Phenylalanine-4-hydroxylase (EC 1.14.16.1) (PAH) (Phe-4-monooxygenase) P00439search (A)
Solvent A
Related entries 1pah, 1tdw, 1lrm
Polymers
Id Name Type UniProt Residues Observed
A Phenylalanine-4-hydroxylase Protein P00439 (PH4H_HUMAN)search
308 100%
Heterogens
Id Name Ligands
A FE (III) ION FE search
A 2-AMINO-6-(1,2-DIHYDROXY-PROPYL)-7,8-DIHYDRO-6H-PTERIDIN-4-ONE H2B search
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