1FVV
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![BU of 1fvv by Molmil](/molmil-images/mine/1fvv) | THE STRUCTURE OF CDK2/CYCLIN A IN COMPLEX WITH AN OXINDOLE INHIBITOR | 分子名称: | 4-[(7-OXO-7H-THIAZOLO[5,4-E]INDOL-8-YLMETHYL)-AMINO]-N-PYRIDIN-2-YL-BENZENESULFONAMIDE, CYCLIN A, CYCLIN-DEPENDENT KINASE 2 | 著者 | Davis, S.T, Benson, B.G, Bramson, H.N, Chapman, D.E, Dickerson, S.H, Dold, K.M, Eberwein, D.J, Edelstein, M, Frye, S.V, Gampe Jr, R.T, Griffin, R.J, Harris, P.A, Hassell, A.M, Holmes, W.D, Hunter, R.N, Knick, V.B, Lackey, K, Lovejoy, B, Luzzio, M.J, Murray, D, Parker, P, Rocque, W.J, Shewchuk, L, Veal, J.M, Walker, D.H, Kuyper, L.K. | 登録日 | 2000-09-20 | 公開日 | 2001-01-17 | 最終更新日 | 2024-02-07 | 実験手法 | X-RAY DIFFRACTION (2.8 Å) | 主引用文献 | Prevention of chemotherapy-induced alopecia in rats by CDK inhibitors. Science, 291, 2001
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7XK8
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![BU of 7xk8 by Molmil](/molmil-images/mine/7xk8) | Cryo-EM structure of the Neuromedin U receptor 2 (NMUR2) in complex with G Protein and its endogeneous Peptide-Agonist NMU25 | 分子名称: | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, Guanine nucleotide-binding protein G(i) subunit alpha-1, ... | 著者 | Zhao, W, Wenru, Z, Mu, W, Minmin, L, Shutian, C, Tingting, T, Gisela, S, Holger, W, Albert, B, Cuiying, Y, Xiaojing, C, Han, S, Wu, B, Zhao, Q. | 登録日 | 2022-04-19 | 公開日 | 2023-02-22 | 実験手法 | ELECTRON MICROSCOPY (3.3 Å) | 主引用文献 | Ligand recognition and activation of neuromedin U receptor 2. Nat Commun, 13, 2022
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1FVR
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![BU of 1fvr by Molmil](/molmil-images/mine/1fvr) | TIE2 KINASE DOMAIN | 分子名称: | TYROSINE-PROTEIN KINASE TIE-2 | 著者 | Shewchuk, L.M, Hassell, A.M, Ellis, B, Holmes, W.D, Davis, R, Horne, E.L, Kadwell, S.H, McKee, D.D, Moore, J.T. | 登録日 | 2000-09-20 | 公開日 | 2001-09-20 | 最終更新日 | 2024-02-07 | 実験手法 | X-RAY DIFFRACTION (2.2 Å) | 主引用文献 | Structure of the Tie2 RTK domain: self-inhibition by the nucleotide binding loop, activation loop, and C-terminal tail. Structure Fold.Des., 8, 2000
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1PV0
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![BU of 1pv0 by Molmil](/molmil-images/mine/1pv0) | Structure of the Sda antikinase | 分子名称: | Sda | 著者 | Rowland, S.L, Burkholder, W.F, Maciejewski, M.W, Grossman, A.D, King, G.F. | 登録日 | 2003-06-26 | 公開日 | 2004-04-13 | 最終更新日 | 2024-05-22 | 実験手法 | SOLUTION NMR | 主引用文献 | Structure and mechanism of Sda: an inhibitor of the histidine kinases that regulate initiation of sporulation in Bacillus subtilis Mol.Cell, 13, 2004
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1P9P
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![BU of 1p9p by Molmil](/molmil-images/mine/1p9p) | The Crystal Structure of a M1G37 tRNA Methyltransferase, TrmD | 分子名称: | S-ADENOSYL-L-HOMOCYSTEINE, tRNA (Guanine-N(1)-)-methyltransferase | 著者 | Elkins, P.A, Watts, J.M, Zalacain, M, Van Thiel, A, Vitaszka, P.R, Redlak, M, Andraos-Selim, C, Rastinejad, F, Holmes, W.M. | 登録日 | 2003-05-12 | 公開日 | 2004-05-18 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (2.5 Å) | 主引用文献 | Insights into Catalysis by a Knotted TrmD tRNA Methyltransferase. J.Mol.Biol., 333, 2003
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4NSV
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![BU of 4nsv by Molmil](/molmil-images/mine/4nsv) | Lysobacter enzymogenes lysc endoproteinase K30R mutant covalently inhibited by TLCK | 分子名称: | CHLORIDE ION, Lysyl endopeptidase, N-[(2S,3S)-7-amino-1-chloro-2-hydroxyheptan-3-yl]-4-methylbenzenesulfonamide (Bound Form), ... | 著者 | Asztalos, P, Muller, A, Holke, W, Sobek, H, Rudolph, M.G. | 登録日 | 2013-11-29 | 公開日 | 2014-04-23 | 最終更新日 | 2023-09-20 | 実験手法 | X-RAY DIFFRACTION (0.9 Å) | 主引用文献 | Atomic resolution structure of a lysine-specific endoproteinase from Lysobacter enzymogenes suggests a hydroxyl group bound to the oxyanion hole. Acta Crystallogr.,Sect.D, 70, 2014
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4NSY
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![BU of 4nsy by Molmil](/molmil-images/mine/4nsy) | Wild-type lysobacter enzymogenes lysc endoproteinase covalently inhibited by TLCK | 分子名称: | CALCIUM ION, CHLORIDE ION, Lysyl endopeptidase, ... | 著者 | Asztalos, P, Muller, A, Holke, W, Sobek, H, Rudolph, M.G. | 登録日 | 2013-11-29 | 公開日 | 2014-04-23 | 最終更新日 | 2023-09-20 | 実験手法 | X-RAY DIFFRACTION (1.1 Å) | 主引用文献 | Atomic resolution structure of a lysine-specific endoproteinase from Lysobacter enzymogenes suggests a hydroxyl group bound to the oxyanion hole. Acta Crystallogr.,Sect.D, 70, 2014
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1C25
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![BU of 1c25 by Molmil](/molmil-images/mine/1c25) | HUMAN CDC25A CATALYTIC DOMAIN | 分子名称: | CDC25A | 著者 | Fauman, E.B, Cogswell, J.P, Lovejoy, B, Rocque, W.J, Holmes, W, Montana, V.G, Piwnica-Worms, H, Rink, M.J, Saper, M.A. | 登録日 | 1998-04-17 | 公開日 | 1998-08-19 | 最終更新日 | 2024-02-07 | 実験手法 | X-RAY DIFFRACTION (2.3 Å) | 主引用文献 | Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A. Cell(Cambridge,Mass.), 93, 1998
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1DKZ
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![BU of 1dkz by Molmil](/molmil-images/mine/1dkz) | THE SUBSTRATE BINDING DOMAIN OF DNAK IN COMPLEX WITH A SUBSTRATE PEPTIDE, DETERMINED FROM TYPE 1 NATIVE CRYSTALS | 分子名称: | SUBSTRATE BINDING DOMAIN OF DNAK, SUBSTRATE PEPTIDE (7 RESIDUES) | 著者 | Zhu, X, Zhao, X, Burkholder, W.F, Gragerov, A, Ogata, C.M, Gottesman, M.E, Hendrickson, W.A. | 登録日 | 1996-06-03 | 公開日 | 1996-12-07 | 最終更新日 | 2024-02-07 | 実験手法 | X-RAY DIFFRACTION (2 Å) | 主引用文献 | Structural analysis of substrate binding by the molecular chaperone DnaK. Science, 272, 1996
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1DKY
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![BU of 1dky by Molmil](/molmil-images/mine/1dky) | THE SUBSTRATE BINDING DOMAIN OF DNAK IN COMPLEX WITH A SUBSTRATE PEPTIDE, DETERMINED FROM TYPE 2 NATIVE CRYSTALS | 分子名称: | DNAK, PEPTIDE SUBSTRATE | 著者 | Zhu, X, Zhao, X, Burkholder, W.F, Gragerov, A, Ogata, C.M, Gottesman, M.E, Hendrickson, W.A. | 登録日 | 1996-06-03 | 公開日 | 1996-12-07 | 最終更新日 | 2024-02-07 | 実験手法 | X-RAY DIFFRACTION (2.8 Å) | 主引用文献 | Structural analysis of substrate binding by the molecular chaperone DnaK. Science, 272, 1996
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1DKX
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![BU of 1dkx by Molmil](/molmil-images/mine/1dkx) | THE SUBSTRATE BINDING DOMAIN OF DNAK IN COMPLEX WITH A SUBSTRATE PEPTIDE, DETERMINED FROM TYPE 1 SELENOMETHIONYL CRYSTALS | 分子名称: | SUBSTRATE BINDING DOMAIN OF DNAK, SUBSTRATE PEPTIDE (7 RESIDUES) | 著者 | Zhu, X, Zhao, X, Burkholder, W.F, Gragerov, A, Ogata, C.M, Gottesman, M.E, Hendrickson, W.A. | 登録日 | 1996-06-03 | 公開日 | 1996-12-07 | 最終更新日 | 2024-02-07 | 実験手法 | X-RAY DIFFRACTION (2 Å) | 主引用文献 | Structural analysis of substrate binding by the molecular chaperone DnaK. Science, 272, 1996
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