4V06
| Crystal structure of human tryptophan hydroxylase 2 (TPH2), catalytic domain | Descriptor: | FE (III) ION, IMIDAZOLE, TRYPTOPHAN 5-HYDROXYLASE 2 | Authors: | Kopec, J, Oberholzer, A, Fitzpatrick, F, Newman, J, Tallant, C, Kiyani, W, Shrestha, L, Burgess-Brown, N, von Delft, F, Arrowsmith, C, Edwards, A, Bountra, C, Yue, W.W. | Deposit date: | 2014-09-11 | Release date: | 2014-10-15 | Last modified: | 2024-01-10 | Method: | X-RAY DIFFRACTION (2.63 Å) | Cite: | Crystal Structure of Human Tryptophane Hydroxylase 2 (Tph2), Catalytic Domain To be Published
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1DMW
| CRYSTAL STRUCTURE OF DOUBLE TRUNCATED HUMAN PHENYLALANINE HYDROXYLASE WITH BOUND 7,8-DIHYDRO-L-BIOPTERIN | Descriptor: | 7,8-DIHYDROBIOPTERIN, FE (III) ION, PHENYLALANINE HYDROXYLASE | Authors: | Erlandsen, H, Stevens, R.C, Flatmark, T. | Deposit date: | 1999-12-15 | Release date: | 2000-03-24 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Crystal structure and site-specific mutagenesis of pterin-bound human phenylalanine hydroxylase. Biochemistry, 39, 2000
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5L01
| Tryptophan 5-hydroxylase in complex with inhibitor (3~{S})-8-[2-azanyl-6-[(1~{R})-1-(4-chloranyl-2-phenyl-phenyl)-2,2,2-tris(fluoranyl)ethoxy]pyrimidin-4-yl]-2,8-diazaspiro[4.5]decane-3-carboxylic acid | Descriptor: | (3~{S})-8-[2-azanyl-6-[(1~{R})-1-(4-chloranyl-2-phenyl-phenyl)-2,2,2-tris(fluoranyl)ethoxy]pyrimidin-4-yl]-2,8-diazaspiro[4.5]decane-3-carboxylic acid, FE (III) ION, Tryptophan 5-hydroxylase 1 | Authors: | Stein, A.J, Goldberg, D.R, De Lombaert, S, Holt, M.C. | Deposit date: | 2016-07-26 | Release date: | 2017-01-25 | Last modified: | 2023-10-04 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Optimization of spirocyclic proline tryptophan hydroxylase-1 inhibitors. Bioorg. Med. Chem. Lett., 27, 2017
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5TPG
| Optimization of spirocyclic proline tryptophanhydroxylase-1 inhibitors | Descriptor: | (3S)-8-(2-amino-6-{(1R)-1-[5-chloro-3'-(methylsulfonyl)[1,1'-biphenyl]-2-yl]-2,2,2-trifluoroethoxy}pyrimidin-4-yl)-2,8-diazaspiro[4.5]decane-3-carboxylic acid, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ACETONITRILE, ... | Authors: | Stein, A.J, Goldberg, D.R, De Lombaert, S, Holt, M.C. | Deposit date: | 2016-10-20 | Release date: | 2017-01-25 | Last modified: | 2024-03-06 | Method: | X-RAY DIFFRACTION (1.5 Å) | Cite: | Optimization of spirocyclic proline tryptophan hydroxylase-1 inhibitors. Bioorg. Med. Chem. Lett., 27, 2017
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5PAH
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6PAH
| HUMAN PHENYLALANINE HYDROXYLASE CATALYTIC DOMAIN DIMER WITH BOUND L-DOPA (3,4-DIHYDROXYPHENYLALANINE) INHIBITOR | Descriptor: | 3,4-DIHYDROXYPHENYLALANINE, FE (III) ION, PHENYLALANINE 4-MONOOXYGENASE | Authors: | Erlandsen, H, Flatmark, T, Stevens, R.C. | Deposit date: | 1998-08-20 | Release date: | 1999-04-27 | Last modified: | 2024-03-13 | Method: | X-RAY DIFFRACTION (2.15 Å) | Cite: | Crystallographic analysis of the human phenylalanine hydroxylase catalytic domain with bound catechol inhibitors at 2.0 A resolution. Biochemistry, 37, 1998
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7VGM
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3PAH
| HUMAN PHENYLALANINE HYDROXYLASE CATALYTIC DOMAIN DIMER WITH BOUND ADRENALINE INHIBITOR | Descriptor: | 4-[(1S)-1-hydroxy-2-(methylamino)ethyl]benzene-1,2-diol, FE (III) ION, PHENYLALANINE HYDROXYLASE | Authors: | Erlandsen, H, Flatmark, T, Stevens, R.C. | Deposit date: | 1998-08-20 | Release date: | 1999-04-27 | Last modified: | 2013-03-20 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Crystallographic analysis of the human phenylalanine hydroxylase catalytic domain with bound catechol inhibitors at 2.0 A resolution. Biochemistry, 37, 1998
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3E2T
| The catalytic domain of chicken tryptophan hydroxylase 1 with bound tryptophan | Descriptor: | FE (III) ION, IMIDAZOLE, SULFATE ION, ... | Authors: | Windahl, M.S, Petersen, C.R, Christensen, H.E.C, Harris, P. | Deposit date: | 2008-08-06 | Release date: | 2008-11-04 | Last modified: | 2023-11-01 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Crystal structure of tryptophan hydroxylase with bound amino acid substrate Biochemistry, 47, 2008
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1PAH
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4PAH
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4JPY
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4JPX
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4Q3Y
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2V28
| Apo structure of the cold active phenylalanine hydroxylase from Colwellia psychrerythraea 34H | Descriptor: | PHENYLALANINE-4-HYDROXYLASE, SULFATE ION | Authors: | Leiros, H.-K.S, Pey, A.L, Innselset, M, Moe, E, Leiros, I, Steen, I.H, Martinez, A. | Deposit date: | 2007-06-04 | Release date: | 2007-06-19 | Last modified: | 2018-10-24 | Method: | X-RAY DIFFRACTION (1.95 Å) | Cite: | Structure of Phenylalanine Hydroxylase from Colwellia Psychrerythraea 34H, a Monomeric Cold Active Enzyme with Local Flexibility Around the Active Site and High Overall Stability. J.Biol.Chem., 282, 2007
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4Q3Z
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2V27
| Structure of the cold active phenylalanine hydroxylase from Colwellia psychrerythraea 34H | Descriptor: | FE (III) ION, PHENYLALANINE HYDROXYLASE, SULFATE ION | Authors: | Leiros, H.-K.S, Pey, A.L, Innselset, M, Moe, E, Leiros, I, Steen, I.H, Martinez, A. | Deposit date: | 2007-06-03 | Release date: | 2007-06-19 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (1.5 Å) | Cite: | Structure of Phenylalanine Hydroxylase from Colwellia Psychrerythraea 34H, a Monomeric Cold Active Enzyme with Local Flexibility Around the Active Site and High Overall Stability. J.Biol.Chem., 282, 2007
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1TG2
| Crystal structure of phenylalanine hydroxylase A313T mutant with 7,8-dihydrobiopterin bound | Descriptor: | 2-AMINO-6-(1,2-DIHYDROXY-PROPYL)-7,8-DIHYDRO-6H-PTERIDIN-4-ONE, FE (III) ION, Phenylalanine-4-hydroxylase | Authors: | 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. | Deposit date: | 2004-05-28 | Release date: | 2004-11-30 | Last modified: | 2023-08-23 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Correction of kinetic and stability defects by tetrahydrobiopterin in phenylketonuria patients with certain phenylalanine hydroxylase mutations. Proc.Natl.Acad.Sci.Usa, 101, 2004
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4Q3W
| Crystal structure of C. violaceum phenylalanine hydroxylase D139E mutation | Descriptor: | 1,2-ETHANEDIOL, COBALT (II) ION, Phenylalanine-4-hydroxylase | Authors: | Ronau, J.A, Abu-Omar, M.M, Das, C. | Deposit date: | 2014-04-12 | Release date: | 2015-02-18 | Last modified: | 2023-09-20 | Method: | X-RAY DIFFRACTION (1.4 Å) | Cite: | A conserved acidic residue in phenylalanine hydroxylase contributes to cofactor affinity and catalysis. Biochemistry, 53, 2014
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4Q3X
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1TDW
| Crystal structure of double truncated human phenylalanine hydroxylase BH4-responsive PKU mutant A313T. | Descriptor: | FE (III) ION, Phenylalanine-4-hydroxylase | Authors: | 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. | Deposit date: | 2004-05-24 | Release date: | 2004-11-30 | Last modified: | 2023-08-23 | Method: | X-RAY DIFFRACTION (2.1 Å) | Cite: | Correction of kinetic and stability defects by tetrahydrobiopterin in phenylketonuria patients with certain phenylalanine hydroxylase mutations. Proc.Natl.Acad.Sci.Usa, 101, 2004
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1TOH
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3HFB
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3HF6
| Crystal structure of human tryptophan hydroxylase type 1 with bound LP-521834 and FE | Descriptor: | 4-(4-amino-6-{[(1R)-1-naphthalen-2-ylethyl]amino}-1,3,5-triazin-2-yl)-L-phenylalanine, FE (III) ION, Tryptophan 5-hydroxylase 1 | Authors: | Tari, L.W, Swanson, R.V, Hunter, M.J. | Deposit date: | 2009-05-11 | Release date: | 2009-11-24 | Last modified: | 2024-02-21 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Mechanism of Inhibition of Novel Tryptophan Hydroxylase Inhibitors Revealed by Co-crystal Structures and Kinetic Analysis Curr Chem Genomics, 4, 2010
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3HF8
| Crystal structure of human tryoptophan hydroxylase type 1 with bound LP-533401 and Fe | Descriptor: | 4-{2-amino-6-[(1R)-2,2,2-trifluoro-1-(3'-fluorobiphenyl-4-yl)ethoxy]pyrimidin-4-yl}-L-phenylalanine, FE (III) ION, Tryptophan 5-hydroxylase 1 | Authors: | Tari, L.W, Swanson, R.V, Hunter, M.J. | Deposit date: | 2009-05-11 | Release date: | 2010-04-21 | Last modified: | 2024-02-21 | Method: | X-RAY DIFFRACTION (1.85 Å) | Cite: | Mechanism of Inhibition of Novel Tryptophan Hydroxylase Inhibitors Revealed by Co-crystal Structures and Kinetic Analysis. Curr Chem Genomics, 4, 2010
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