4L69
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7UOW
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7F8R
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6AVN
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6B0N
| Crystal structure of the cleavage-independent prefusion HIV Env glycoprotein trimer of the clade A BG505 isolate (NFL construct) in complex with Fabs PGT122 and PGV19 at 3.39 A | 分子名称: | 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, Envelope glycoprotein gp140, ... | 著者 | Sarkar, A, Irimia, A, Wilson, I.A. | 登録日 | 2017-09-14 | 公開日 | 2018-05-30 | 最終更新日 | 2023-10-04 | 実験手法 | X-RAY DIFFRACTION (3.4 Å) | 主引用文献 | Structure of a cleavage-independent HIV Env recapitulates the glycoprotein architecture of the native cleaved trimer. Nat Commun, 9, 2018
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8E7E
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4OW8
| Crystal structure of kinase domain of PknA from Mtb | 分子名称: | GLYCEROL, SULFATE ION, Serine/threonine-protein kinase PknA | 著者 | Ravala, S.K, Singh, S, Yadav, G.S, Karthikeyan, S, Chakraborti, P.K. | 登録日 | 2014-01-31 | 公開日 | 2015-02-04 | 最終更新日 | 2023-09-27 | 実験手法 | X-RAY DIFFRACTION (2.03 Å) | 主引用文献 | Evidence that phosphorylation of threonine in the GT motif triggers activation of PknA, a eukaryotic-type serine/threonine kinase from Mycobacterium tuberculosis. Febs J., 282, 2015
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6JHU
| Crystal Structure Of Biotin Protein Ligase From Leishmania Major in complex with Biotinyl-5-AMP | 分子名称: | BIOTINYL-5-AMP, Biotin/lipoate protein ligase-like protein, SULFATE ION | 著者 | Rajak, M, Patel, A, Sundd, M. | 登録日 | 2019-02-19 | 公開日 | 2020-04-08 | 最終更新日 | 2023-11-22 | 実験手法 | X-RAY DIFFRACTION (1.97 Å) | 主引用文献 | Leishmania major biotin protein ligase forms a unique cross-handshake dimer Acta Crystallogr.,Sect.D, 77, 2021
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6KJM
| Structural basis for domain rotation during adenylation of active site K123 and fragment library screening against NAD+ -dependent DNA ligase from Mycobacterium tuberculosis | 分子名称: | ADENOSINE MONOPHOSPHATE, BETA-NICOTINAMIDE RIBOSE MONOPHOSPHATE, DNA ligase A, ... | 著者 | Ramachandran, R, Shukla, A, Afsar, M. | 登録日 | 2019-07-22 | 公開日 | 2020-07-22 | 最終更新日 | 2023-11-22 | 実験手法 | X-RAY DIFFRACTION (2.2 Å) | 主引用文献 | Structure based identification of first-in-class fragment inhibitors that target the NMN pocket of M. tuberculosis NAD + -dependent DNA ligase A. J.Struct.Biol., 213, 2021
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6KKV
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8E7J
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7DBS
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4FOP
| Crystal Structure of Peptidyl-tRNA hydrolase from Acinetobacter baumannii at 1.86 A resolution | 分子名称: | ACETATE ION, DI(HYDROXYETHYL)ETHER, GLYCEROL, ... | 著者 | Kaushik, S, Kumar, S, Singh, N, Sinha, M, Kaur, P, Sharma, S, Singh, T.P. | 登録日 | 2012-06-21 | 公開日 | 2012-07-04 | 最終更新日 | 2023-11-08 | 実験手法 | X-RAY DIFFRACTION (1.86 Å) | 主引用文献 | The Mode of Inhibitor Binding to Peptidyl-tRNA Hydrolase: Binding Studies and Structure Determination of Unbound and Bound Peptidyl-tRNA Hydrolase from Acinetobacter baumannii Plos One, 8, 2013
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1NID
| THE STRUCTURE OF CU-NITRITE REDUCTASE FROM ACHROMOBACTER CYCLOCLASTES AT FIVE PH VALUES, WITH NITRITE BOUND AND WITH TYPE II CU DEPLETED | 分子名称: | COPPER (II) ION, NITRITE ION, NITRITE REDUCTASE | 著者 | Adman, E.T, Godden, J.W, Turley, S. | 登録日 | 1995-07-03 | 公開日 | 1995-12-07 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (2.2 Å) | 主引用文献 | The structure of copper-nitrite reductase from Achromobacter cycloclastes at five pH values, with NO2- bound and with type II copper depleted. J.Biol.Chem., 270, 1995
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1NIA
| THE STRUCTURE OF CU-NITRITE REDUCTASE FROM ACHROMOBACTER CYCLOCLASTES AT FIVE PH VALUES, WITH NITRITE BOUND AND WITH TYPE II CU DEPLETED | 分子名称: | COPPER (II) ION, NITRITE REDUCTASE | 著者 | Adman, E.T, Godden, J.W, Turley, S. | 登録日 | 1995-07-03 | 公開日 | 1995-12-07 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (2.5 Å) | 主引用文献 | The structure of copper-nitrite reductase from Achromobacter cycloclastes at five pH values, with NO2- bound and with type II copper depleted. J.Biol.Chem., 270, 1995
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1NIC
| THE STRUCTURE OF CU-NITRITE REDUCTASE FROM ACHROMOBACTER CYCLOCLASTES AT FIVE PH VALUES, WITH NITRITE BOUND AND WITH TYPE II CU DEPLETED | 分子名称: | COPPER (II) ION, NITRITE REDUCTASE, SULFATE ION | 著者 | Adman, E.T, Godden, J.W, Turley, S. | 登録日 | 1995-07-03 | 公開日 | 1995-12-07 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (1.9 Å) | 主引用文献 | The structure of copper-nitrite reductase from Achromobacter cycloclastes at five pH values, with NO2- bound and with type II copper depleted. J.Biol.Chem., 270, 1995
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1NIB
| THE STRUCTURE OF CU-NITRITE REDUCTASE FROM ACHROMOBACTER CYCLOCLASTES AT FIVE PH VALUES, WITH NITRITE BOUND AND WITH TYPE II CU DEPLETED | 分子名称: | COPPER (II) ION, NITRITE REDUCTASE | 著者 | Adman, E.T, Godden, J.W, Turley, S. | 登録日 | 1995-07-03 | 公開日 | 1995-12-07 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (2.7 Å) | 主引用文献 | The structure of copper-nitrite reductase from Achromobacter cycloclastes at five pH values, with NO2- bound and with type II copper depleted. J.Biol.Chem., 270, 1995
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1NIE
| THE STRUCTURE OF CU-NITRITE REDUCTASE FROM ACHROMOBACTER CYCLOCLASTES AT FIVE PH VALUES, WITH NITRITE BOUND AND WITH TYPE II CU DEPLETED | 分子名称: | COPPER (II) ION, NITRITE REDUCTASE | 著者 | Adman, E.T, Godden, J.W, Turley, S. | 登録日 | 1995-07-03 | 公開日 | 1995-12-07 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (1.9 Å) | 主引用文献 | The structure of copper-nitrite reductase from Achromobacter cycloclastes at five pH values, with NO2- bound and with type II copper depleted. J.Biol.Chem., 270, 1995
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1NIF
| THE STRUCTURE OF CU-NITRITE REDUCTASE FROM ACHROMOBACTER CYCLOCLASTES AT FIVE PH VALUES, WITH NITRITE BOUND AND WITH TYPE II CU DEPLETED | 分子名称: | COPPER (II) ION, NITRITE REDUCTASE | 著者 | Adman, E.T, Godden, J.W, Turley, S. | 登録日 | 1995-07-03 | 公開日 | 1995-12-07 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (1.7 Å) | 主引用文献 | The structure of copper-nitrite reductase from Achromobacter cycloclastes at five pH values, with NO2- bound and with type II copper depleted. J.Biol.Chem., 270, 1995
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7D96
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7D97
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6JP9
| Crsytal structure of a XMP complexed ATPPase subunit of M. jannaschii GMP synthetase | 分子名称: | GMP synthase [glutamine-hydrolyzing] subunit B, MALONIC ACID, TRIETHYLENE GLYCOL, ... | 著者 | Shivakumarasamy, S, Balaram, H. | 登録日 | 2019-03-26 | 公開日 | 2020-04-22 | 最終更新日 | 2023-11-29 | 実験手法 | X-RAY DIFFRACTION (2.1 Å) | 主引用文献 | Mechanistic Insights into the Functioning of a Two-Subunit GMP Synthetase, an Allosterically Regulated, Ammonia Channeling Enzyme. Biochemistry, 61, 2022
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3SPX
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3TBH
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3T4P
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