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PDBe Entry: 1tg2 
Crystal structure of phenylalanine hydroxylase A313T mutant with 7,8-dihydrobiopterin bound
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OXIDOREDUCTASE
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X-RAY DIFFRACTION
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Resolution: 2.2 Å, R-factor: 21.3%, Free R-factor: 25.4%, Spacegroup: C 2 2 21
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30/11/2004, deposition: 28/05/2004, last revision: 24/02/2009
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Erlandsen, H. ; Pey, A.L. ; Gamez, A. ; Perez, B. ; Desviat, L.R. ; Aguado, C. ; Koch, R. ; Surendran, S. ; Tyring, S. ; Matalon, R. ; Scriver, C.R. ; Ugarte, M. ; Martinez, A. ; Stevens, R.C.
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Correction of kinetic and stability defects by tetrahydrobiopterin in phenylketonuria patients with certain phenylalanine hydroxylase mutations. PROC.NATL.ACAD.SCI.USA vol:101, pag:16903-16908 (2004) [PubMed ID 15557004 ]
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phenylalanine hydroxylase phenylketonuria mutant A313T in complex with cofactor analogue 7 , 8-dihydrobiopterin , OXIDOREDUCTASE
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1.14.16.1 ExPASy BRENDA (A)
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Homo sapiens(human) 9606 (A)
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Phenylalanine-4-hydroxylase (EC 1.14.16.1) (PAH) (Phe-4-monooxygenase) P00439 (A)
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A
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1pah, 1tdw, 1lrm
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| A |
Phenylalanine-4-hydroxylase |
Protein |
P00439 (PH4H_HUMAN)
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308 |
100% |
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| A |
FE (III) ION |
FE
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| A |
2-AMINO-6-(1,2-DIHYDROXY-PROPYL)-7,8-DIHYDRO-6H-PTERIDIN-4-ONE |
H2B
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