1JD3
| Chorismate lyase G90A mutant with bound product | 分子名称: | P-HYDROXYBENZOIC ACID, chorismate lyase | 著者 | Mayhew, M, Smith, N, Holden, M.J, Gallagher, D.T. | 登録日 | 2001-06-12 | 公開日 | 2001-06-20 | 最終更新日 | 2023-08-16 | 実験手法 | X-RAY DIFFRACTION (2.03 Å) | 主引用文献 | Structural analysis of ligand binding and catalysis in chorismate lyase. Arch.Biochem.Biophys., 445, 2006
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1IXA
| THE THREE-DIMENSIONAL STRUCTURE OF THE FIRST EGF-LIKE MODULE OF HUMAN FACTOR IX: COMPARISON WITH EGF AND TGF-A | 分子名称: | EGF-LIKE MODULE OF HUMAN FACTOR IX | 著者 | Baron, M, Norman, D.G, Harvey, T.S, Hanford, P.A, Mayhew, M, Tse, A.G.D, Brownlee, G.G, Campbell, I.D.C. | 登録日 | 1991-11-14 | 公開日 | 1993-10-31 | 最終更新日 | 2022-02-23 | 実験手法 | SOLUTION NMR | 主引用文献 | The three-dimensional structure of the first EGF-like module of human factor IX: comparison with EGF and TGF-alpha. Protein Sci., 1, 1992
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1R7S
| PUTIDAREDOXIN (Fe2S2 ferredoxin), C73G mutant | 分子名称: | FE2/S2 (INORGANIC) CLUSTER, Putidaredoxin | 著者 | Smith, N, Mayhew, M, Kelly, H, Robinson, H, Heroux, A, Holden, M.J, Gallagher, D.T. | 登録日 | 2003-10-22 | 公開日 | 2004-04-27 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (1.91 Å) | 主引用文献 | Structure of C73G putidaredoxin from Pseudomonas putida. Acta Crystallogr.,Sect.D, 60, 2004
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1G1B
| CHORISMATE LYASE (WILD-TYPE) WITH BOUND PRODUCT | 分子名称: | CHORISMATE LYASE, P-HYDROXYBENZOIC ACID | 著者 | Gallagher, D.T, Mayhew, M, Holden, M.J, Kim, K.J, Howard, A, Vilker, V.L. | 登録日 | 2000-10-11 | 公開日 | 2001-04-11 | 最終更新日 | 2024-02-07 | 実験手法 | X-RAY DIFFRACTION (1.99 Å) | 主引用文献 | The crystal structure of chorismate lyase shows a new fold and a tightly retained product. Proteins, 44, 2001
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1TT8
| CHORISMATE LYASE WITH PRODUCT, 1.0 A RESOLUTION | 分子名称: | Chorismate-pyruvate lyase, P-HYDROXYBENZOIC ACID | 著者 | Gallagher, D.T, Mayhew, M, Holden, M.J, Vilker, V, Howard, A. | 登録日 | 2004-06-22 | 公開日 | 2004-12-28 | 最終更新日 | 2023-08-23 | 実験手法 | X-RAY DIFFRACTION (1 Å) | 主引用文献 | Structural analysis of ligand binding and catalysis in chorismate lyase. Arch.Biochem.Biophys., 445, 2006
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1EDM
| EPIDERMAL GROWTH FACTOR-LIKE DOMAIN FROM HUMAN FACTOR IX | 分子名称: | CALCIUM ION, FACTOR IX | 著者 | Rao, Z, Handford, P, Mayhew, M, Knott, V, Brownlee, G.G, Stuart, D. | 登録日 | 1996-03-21 | 公開日 | 1996-10-14 | 最終更新日 | 2024-10-09 | 実験手法 | X-RAY DIFFRACTION (1.5 Å) | 主引用文献 | The structure of a Ca(2+)-binding epidermal growth factor-like domain: its role in protein-protein interactions. Cell(Cambridge,Mass.), 82, 1995
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1FW9
| CHORISMATE LYASE WITH BOUND PRODUCT | 分子名称: | CHORISMATE LYASE, P-HYDROXYBENZOIC ACID | 著者 | Gallagher, D.T, Mayhew, M, Holden, M, Vilker, V, Howard, A. | 登録日 | 2000-09-22 | 公開日 | 2001-03-22 | 最終更新日 | 2024-02-07 | 実験手法 | X-RAY DIFFRACTION (1.4 Å) | 主引用文献 | The crystal structure of chorismate lyase shows a new fold and a tightly retained product. Proteins, 44, 2001
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1G81
| CHORISMATE LYASE WITH BOUND PRODUCT, ORTHORHOMBIC CRYSTAL FORM | 分子名称: | CHORISMATE LYASE, P-HYDROXYBENZOIC ACID | 著者 | Gallagher, D.T, Mayhew, M, Holden, M.J, Vilker, V.L, Howard, A. | 登録日 | 2000-11-15 | 公開日 | 2001-05-15 | 最終更新日 | 2024-02-07 | 実験手法 | X-RAY DIFFRACTION (1.71 Å) | 主引用文献 | The crystal structure of chorismate lyase shows a new fold and a tightly retained product. Proteins, 44, 2001
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1XLR
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2AHC
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1OMO
| alanine dehydrogenase dimer w/bound NAD (archaeal) | 分子名称: | NICOTINAMIDE-ADENINE-DINUCLEOTIDE, SODIUM ION, alanine dehydrogenase | 著者 | Gallagher, D.T, Smith, N.N, Holden, M.J, Schroeder, I, Monbouquette, H.G. | 登録日 | 2003-02-25 | 公開日 | 2004-07-06 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (2.32 Å) | 主引用文献 | Structure of alanine dehydrogenase from Archaeoglobus: active site analysis and relation to bacterial cyclodeaminases and mammalian mu crystallin. J.Mol.Biol., 342, 2004
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1BF9
| N-TERMINAL EGF-LIKE DOMAIN FROM HUMAN FACTOR VII, NMR, 23 STRUCTURES | 分子名称: | FACTOR VII | 著者 | Muranyi, A, Finn, B.E, Gippert, G.P, Forsen, S, Stenflo, J, Drakenberg, T. | 登録日 | 1998-05-28 | 公開日 | 1999-02-16 | 最終更新日 | 2017-11-29 | 実験手法 | SOLUTION NMR | 主引用文献 | Solution structure of the N-terminal EGF-like domain from human factor VII. Biochemistry, 37, 1998
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