1XDN
| High resolution crystal structure of an editosome enzyme from trypanosoma brucei: RNA editing ligase 1 | 分子名称: | ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, RNA editing ligase MP52 | 著者 | Deng, J, Schnaufer, A, Salavati, R, Stuart, K.D, Hol, W.G. | 登録日 | 2004-09-07 | 公開日 | 2004-12-07 | 最終更新日 | 2014-09-10 | 実験手法 | X-RAY DIFFRACTION (1.2 Å) | 主引用文献 | High resolution crystal structure of a key editosome enzyme from Trypanosoma brucei: RNA editing ligase 1. J.Mol.Biol., 343, 2004
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2A0U
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1Y63
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1Y13
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2B30
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1LTI
| HEAT-LABILE ENTEROTOXIN (LT-I) COMPLEX WITH T-ANTIGEN | 分子名称: | HEAT LABILE ENTEROTOXIN TYPE I, beta-D-galactopyranose, beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-alpha-D-galactopyranose | 著者 | Van Den Akker, F, Hol, W.G.J. | 登録日 | 1996-05-09 | 公開日 | 1996-08-17 | 最終更新日 | 2020-07-29 | 実験手法 | X-RAY DIFFRACTION (2.13 Å) | 主引用文献 | Tumor marker disaccharide D-Gal-beta 1, 3-GalNAc complexed to heat-labile enterotoxin from Escherichia coli. Protein Sci., 5, 1996
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1JVZ
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2B4V
| Structural Basis for UTP Specificity of RNA Editing TUTases From Trypanosoma Brucei | 分子名称: | POTASSIUM ION, RNA editing complex protein MP57 | 著者 | Deng, J, Ernst, N.L, Turley, S, Stuart, K.D, Hol, W.G. | 登録日 | 2005-09-26 | 公開日 | 2005-11-22 | 最終更新日 | 2021-10-20 | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | 主引用文献 | Structural basis for UTP specificity of RNA editing TUTases from Trypanosoma brucei. Embo J., 24, 2005
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2B56
| Structural Basis for UTP Specificity of RNA Editing TUTases From Trypanosoma Brucei | 分子名称: | MAGNESIUM ION, RNA editing complex protein MP57, URIDINE 5'-TRIPHOSPHATE, ... | 著者 | Deng, J, Ernst, N.L, Turley, S, Stuart, K.D, Hol, W.G. | 登録日 | 2005-09-27 | 公開日 | 2005-11-22 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (1.97 Å) | 主引用文献 | Structural basis for UTP specificity of RNA editing TUTases from Trypanosoma brucei. Embo J., 24, 2005
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2B94
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2B51
| Structural Basis for UTP Specificity of RNA Editing TUTases from Trypanosoma Brucei | 分子名称: | MANGANESE (II) ION, RNA editing complex protein MP57, URIDINE 5'-TRIPHOSPHATE | 著者 | Deng, J, Ernst, N.L, Turley, S, Stuart, K.D, Hol, W.G. | 登録日 | 2005-09-27 | 公開日 | 2005-11-22 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (2.05 Å) | 主引用文献 | Structural basis for UTP specificity of RNA editing TUTases from Trypanosoma brucei. Embo J., 24, 2005
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1XQ9
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1Y1X
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1IIH
| STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TRIOSEPHOSPHATE ISOMERASE COMPLEXED WITH 3-PHOSPHOGLYCERATE | 分子名称: | 3-PHOSPHOGLYCERIC ACID, TRIOSEPHOSPHATE ISOMERASE | 著者 | Noble, M.E, Wierenga, R.K, Lambeir, A.M, Opperdoes, F.R, Thunnissen, A.M, Kalk, K.H, Groendijk, H, Hol, W.G.J. | 登録日 | 2001-04-23 | 公開日 | 2001-05-11 | 最終更新日 | 2024-02-07 | 実験手法 | X-RAY DIFFRACTION (2.2 Å) | 主引用文献 | The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes. Proteins, 10, 1991
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2DTR
| STRUCTURE OF DIPHTHERIA TOXIN REPRESSOR | 分子名称: | COBALT (II) ION, DIPHTHERIA TOXIN REPRESSOR, SULFATE ION | 著者 | Qiu, X, Pohl, E, Hol, W.G. | 登録日 | 1996-07-26 | 公開日 | 1997-08-20 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (1.9 Å) | 主引用文献 | High-resolution structure of the diphtheria toxin repressor complexed with cobalt and manganese reveals an SH3-like third domain and suggests a possible role of phosphate as co-corepressor. Biochemistry, 35, 1996
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2F84
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1NHQ
| CRYSTALLOGRAPHIC ANALYSES OF NADH PEROXIDASE CYS42ALA AND CYS42SER MUTANTS: ACTIVE SITE STRUCTURE, MECHANISTIC IMPLICATIONS, AND AN UNUSUAL ENVIRONMENT OF ARG303 | 分子名称: | FLAVIN-ADENINE DINUCLEOTIDE, NADH PEROXIDASE, SULFATE ION | 著者 | Mande, S.S, Claiborne, A, Hol, W.G.J. | 登録日 | 1994-12-09 | 公開日 | 1995-02-14 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (2 Å) | 主引用文献 | Crystallographic analyses of NADH peroxidase Cys42Ala and Cys42Ser mutants: active site structures, mechanistic implications, and an unusual environment of Arg 303. Biochemistry, 34, 1995
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1NHP
| CRYSTALLOGRAPHIC ANALYSES OF NADH PEROXIDASE CYS42ALA AND CYS42SER MUTANTS: ACTIVE SITE STRUCTURE, MECHANISTIC IMPLICATIONS, AND AN UNUSUAL ENVIRONMENT OF ARG303 | 分子名称: | FLAVIN-ADENINE DINUCLEOTIDE, NADH PEROXIDASE, SULFATE ION | 著者 | Mande, S.S, Claiborne, A, Hol, W.G.J. | 登録日 | 1994-12-09 | 公開日 | 1995-02-14 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (2 Å) | 主引用文献 | Crystallographic analyses of NADH peroxidase Cys42Ala and Cys42Ser mutants: active site structures, mechanistic implications, and an unusual environment of Arg 303. Biochemistry, 34, 1995
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1NHS
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1NHR
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1QS0
| Crystal Structure of Pseudomonas Putida 2-oxoisovalerate Dehydrogenase (Branched-Chain Alpha-Keto Acid Dehydrogenase, E1B) | 分子名称: | 2-OXO-4-METHYLPENTANOIC ACID, 2-OXOISOVALERATE DEHYDROGENASE ALPHA-SUBUNIT, 2-OXOISOVALERATE DEHYDROGENASE BETA-SUBUNIT, ... | 著者 | Aevarsson, A, Seger, K, Turley, S, Sokatch, J.R, Hol, W.G.J. | 登録日 | 1999-06-24 | 公開日 | 1999-08-18 | 最終更新日 | 2021-08-04 | 実験手法 | X-RAY DIFFRACTION (2.4 Å) | 主引用文献 | Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes. Nat.Struct.Biol., 6, 1999
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1QCB
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1QB5
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1RL4
| Plasmodium falciparum peptide deformylase complex with inhibitor | 分子名称: | (2R)-2-{[FORMYL(HYDROXY)AMINO]METHYL}HEXANOIC ACID, 2-{N'-[2-(5-AMINO-1-PHENYLCARBAMOYL-PENTYLCARBAMOYL)-HEXYL]-HYDRAZINOMETHYL}-HEXANOIC ACID(5-AMINO-1-PHENYLCARBAMOYL-PENTYL)-AMIDE, COBALT (II) ION, ... | 著者 | Robien, M.A, Nguyen, K.T, Kumar, A, Hirsh, I, Turley, S, Pei, D, Hol, W.G.J. | 登録日 | 2003-11-24 | 公開日 | 2003-12-09 | 最終更新日 | 2023-08-23 | 実験手法 | X-RAY DIFFRACTION (2.18 Å) | 主引用文献 | An improved crystal form of Plasmodium falciparum peptide deformylase. Protein Sci., 13, 2004
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1R49
| Human topoisomerase I (Topo70) double mutant K532R/Y723F | 分子名称: | 5'-D(*AP*AP*AP*AP*AP*GP*AP*CP*TP*TP*AP*GP*AP*AP*AP*AP*AP*TP*TP*TP*TP*T)-3', 5'-D(P*AP*AP*AP*AP*AP*TP*TP*TP*TP*TP*CP*TP*AP*AP*GP*TP*CP*TP*TP*TP*TP*T)-3', DNA topoisomerase I | 著者 | Interthal, H, Quigley, P.M, Hol, W.G, Champoux, J.J. | 登録日 | 2003-10-03 | 公開日 | 2003-12-16 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (3.13 Å) | 主引用文献 | The role of lysine 532 in the catalytic mechanism of human topoisomerase I. J.Biol.Chem., 279, 2004
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