1Y66
 
 | | Dioxane contributes to the altered conformation and oligomerization state of a designed engrailed homeodomain variant | | 分子名称: | 1,4-DIETHYLENE DIOXIDE, ACETIC ACID, CADMIUM ION, ... | | 著者 | Hom, G.K, Lassila, J.K, Thomas, L.M, Mayo, S.L. | | 登録日 | 2004-12-03 | | 公開日 | 2005-03-15 | | 最終更新日 | 2024-02-14 | | 実験手法 | X-RAY DIFFRACTION (1.65 Å) | | 主引用文献 | Dioxane contributes to the altered conformation and oligomerization state of a designed engrailed homeodomain variant.
Protein Sci., 14, 2005
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2P6J
 | | Full-sequence computational design and solution structure of a thermostable protein variant | | 分子名称: | designed engrailed homeodomain variant UVF | | 著者 | Shah, P.S, Hom, G.K, Ross, S.A, Lassila, J.K, Crowhurst, K.A, Mayo, S.L. | | 登録日 | 2007-03-18 | | 公開日 | 2007-08-14 | | 最終更新日 | 2024-05-22 | | 実験手法 | SOLUTION NMR | | 主引用文献 | Full-sequence Computational Design and Solution Structure of a Thermostable Protein Variant.
J.Mol.Biol., 372, 2007
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3CMR
 | | E. coli alkaline phosphatase mutant R166S in complex with phosphate | | 分子名称: | Alkaline phosphatase, MAGNESIUM ION, PHOSPHATE ION, ... | | 著者 | O'Brien, P.J, Lassila, J.K, Fenn, T.D, Zalatan, J.G, Herschlag, D. | | 登録日 | 2008-03-24 | | 公開日 | 2008-07-29 | | 最終更新日 | 2023-08-30 | | 実験手法 | X-RAY DIFFRACTION (2.05 Å) | | 主引用文献 | Arginine coordination in enzymatic phosphoryl transfer: evaluation of the effect of Arg166 mutations in Escherichia coli alkaline phosphatase
Biochemistry, 47, 2008
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3TG0
 | | E. coli alkaline phosphatase with bound inorganic phosphate | | 分子名称: | Alkaline phosphatase, MAGNESIUM ION, PHOSPHATE ION, ... | | 著者 | Bobyr, E, Lassila, J.K, Wiersma-Koch, H.I, Fenn, T.D, Lee, J.J, Nikolic-Hughes, I, Hodgson, K.O, Rees, D.C, Hedman, B, Herschlag, D. | | 登録日 | 2011-08-16 | | 公開日 | 2011-11-09 | | 最終更新日 | 2023-09-13 | | 実験手法 | X-RAY DIFFRACTION (1.2 Å) | | 主引用文献 | High-resolution analysis of Zn(2+) coordination in the alkaline phosphatase superfamily by EXAFS and x-ray crystallography.
J.Mol.Biol., 415, 2012
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3NXF
 | | Robust computational design, optimization, and structural characterization of retroaldol enzymes | | 分子名称: | Retro-Aldolase, SULFATE ION | | 著者 | Althoff, E.A, Jiang, L, Wang, L, Lassila, J.K, Moody, J, Bolduc, J, Wang, Z.Z, Smith, M, Hari, S, Herschlag, D, Stoddard, B.L, Baker, D. | | 登録日 | 2010-07-13 | | 公開日 | 2011-06-29 | | 最終更新日 | 2023-09-06 | | 実験手法 | X-RAY DIFFRACTION (2.4 Å) | | 主引用文献 | Structural analyses of covalent enzyme-substrate analog complexes reveal strengths and limitations of de novo enzyme design.
J.Mol.Biol., 415, 2012
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3O6Y
 | | Robust computational design, optimization, and structural characterization of retroaldol enzymes | | 分子名称: | Retro-Aldolase, SULFATE ION | | 著者 | Althoff, E.A, Wang, L, Jiang, L, Moody, J, Bolduc, J, Lassila, J.K, Wang, Z.Z, Smith, M, Hari, S, Herschlag, D, Stoddard, B.L, Baker, D. | | 登録日 | 2010-07-29 | | 公開日 | 2011-06-29 | | 最終更新日 | 2023-09-06 | | 実験手法 | X-RAY DIFFRACTION (2.091 Å) | | 主引用文献 | Structural analyses of covalent enzyme-substrate analog complexes reveal strengths and limitations of de novo enzyme design.
J.Mol.Biol., 415, 2012
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3UD6
 | | Structural analyses of covalent enzyme-substrate analogue complexes reveal strengths and limitations of de novo enzyme design | | 分子名称: | 1-(6-METHOXYNAPHTHALEN-2-YL)BUTANE-1,3-DIONE, RETRO-ALDOLASE, SULFATE ION | | 著者 | Baker, D, Stoddard, B.L, Althoff, E.A, Wang, L, Jiang, L, Moody, J, Bolduc, J, Lassila, J, Hilvert, D. | | 登録日 | 2011-10-27 | | 公開日 | 2011-11-23 | | 最終更新日 | 2023-09-13 | | 実験手法 | X-RAY DIFFRACTION (2.091 Å) | | 主引用文献 | Structural analyses of covalent enzyme-substrate analog complexes reveal strengths and limitations of de novo enzyme design.
J.Mol.Biol., 415, 2012
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4L7K
 | | Crystal Structure of Ketosteroid Isomerase D38E from Pseudomonas Testosteroni (tKSI) | | 分子名称: | GLYCEROL, SULFATE ION, Steroid Delta-isomerase | | 著者 | Gonzalez, A, Tsai, Y, Schwans, J, Sunden, F, Herschlag, D. | | 登録日 | 2013-06-14 | | 公開日 | 2013-07-03 | | 最終更新日 | 2024-02-28 | | 実験手法 | X-RAY DIFFRACTION (2.1 Å) | | 主引用文献 | Use of anion-aromatic interactions to position the general base in the ketosteroid isomerase active site.
Proc.Natl.Acad.Sci.USA, 110, 2013
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