3BFP
 
 | | Crystal Structure of apo-PglD from Campylobacter jejuni | | 分子名称: | Acetyltransferase, CITRATE ANION | | 著者 | Rangarajan, E.S, Watson, D.C, Leclerc, S, Proteau, A, Cygler, M, Matte, A, Young, N.M, Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) | | 登録日 | 2007-11-22 | | 公開日 | 2008-01-22 | | 最終更新日 | 2024-02-21 | | 実験手法 | X-RAY DIFFRACTION (1.75 Å) | | 主引用文献 | Structure and Active Site Residues of PglD, an N-Acetyltransferase from the Bacillosamine Synthetic Pathway Required for N-Glycan Synthesis in Campylobacter jejuni.
Biochemistry, 47, 2008
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1TSZ
 | | THYMIDYLATE SYNTHASE R179K MUTANT | | 分子名称: | PHOSPHATE ION, THYMIDYLATE SYNTHASE | | 著者 | Finer-Moore, J, Stroud, R.M. | | 登録日 | 1995-12-05 | | 公開日 | 1996-03-08 | | 最終更新日 | 2024-02-14 | | 実験手法 | X-RAY DIFFRACTION (2.75 Å) | | 主引用文献 | Contribution of a salt bridge to binding affinity and dUMP orientation to catalytic rate: mutation of a substrate-binding arginine in thymidylate synthase.
Protein Eng., 9, 1996
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1TSW
 | | THYMIDYLATE SYNTHASE R179A MUTANT | | 分子名称: | PHOSPHATE ION, THYMIDYLATE SYNTHASE | | 著者 | Finer-Moore, J, Stroud, R.M. | | 登録日 | 1995-12-05 | | 公開日 | 1996-03-08 | | 最終更新日 | 2024-02-14 | | 実験手法 | X-RAY DIFFRACTION (2.5 Å) | | 主引用文献 | Contribution of a salt bridge to binding affinity and dUMP orientation to catalytic rate: mutation of a substrate-binding arginine in thymidylate synthase.
Protein Eng., 9, 1996
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4JAV
 | | Structural basis of a rationally rewired protein-protein interface (HK853wt and RR468mutant V13P, L14I, I17M and N21V) | | 分子名称: | ADENOSINE-5'-DIPHOSPHATE, CHLORIDE ION, Histidine kinase, ... | | 著者 | Podgornaia, A.I, Casino, P, Marina, A, Laub, M.T. | | 登録日 | 2013-02-19 | | 公開日 | 2013-09-04 | | 最終更新日 | 2023-11-08 | | 実験手法 | X-RAY DIFFRACTION (3.1 Å) | | 主引用文献 | Structural basis of a rationally rewired protein-protein interface critical to bacterial signaling
Structure, 21, 2013
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3BGX
 | | E. coli Thymidylate Synthase C146S mutant complexed with dTMP and MTF | | 分子名称: | N-({4-[(6aR)-3-amino-1-oxo-1,2,5,6,6a,7-hexahydroimidazo[1,5-f]pteridin-8(9H)-yl]phenyl}carbonyl)-L-glutamic acid, SULFATE ION, THYMIDINE-5'-PHOSPHATE, ... | | 著者 | Roberts, S.A, Montfort, W.R. | | 登録日 | 2007-11-27 | | 公開日 | 2008-12-09 | | 最終更新日 | 2021-10-20 | | 実験手法 | X-RAY DIFFRACTION (1.93 Å) | | 主引用文献 | Structural Studies of Early Events in Catalysis by Thymidylate Synthase
To be Published
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6Q11
 | | Crystal structure of MurA from Clostridium difficile, mutation C116S, in the presence of URIDINE-DIPHOSPHATE-2(N-ACETYLGLUCOSAMINYL) BUTYRIC ACID | | 分子名称: | 1,2-ETHANEDIOL, SODIUM ION, UDP-N-acetylglucosamine 1-carboxyvinyltransferase, ... | | 著者 | Dopkins, B.J, Call, C.J, Thoden, J.B, Holden, H.M. | | 登録日 | 2019-08-02 | | 公開日 | 2019-11-27 | | 最終更新日 | 2023-10-11 | | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | | 主引用文献 | Crystal structure of MurA from Clostridium difficile, mutation C116S, in the presence of URIDINE-DIPHOSPHATE-2(N-ACETYLGLUCOSAMINYL) BUTYRIC ACID
To Be Published
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5WRN
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1TSL
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1TSM
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1KNY
 | | KANAMYCIN NUCLEOTIDYLTRANSFERASE | | 分子名称: | DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER, KANAMYCIN A, KANAMYCIN NUCLEOTIDYLTRANSFERASE, ... | | 著者 | Pedersen, L.C, Benning, M.M, Holden, H.M. | | 登録日 | 1995-07-07 | | 公開日 | 1996-08-17 | | 最終更新日 | 2024-02-14 | | 実験手法 | X-RAY DIFFRACTION (2.5 Å) | | 主引用文献 | Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase.
Biochemistry, 34, 1995
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4NSQ
 | | Crystal structure of PCAF | | 分子名称: | COENZYME A, Histone acetyltransferase KAT2B | | 著者 | Lin, J.Y, Cai, Y.F. | | 登録日 | 2013-11-28 | | 公開日 | 2014-03-05 | | 最終更新日 | 2024-02-28 | | 実験手法 | X-RAY DIFFRACTION (2.3108 Å) | | 主引用文献 | Dimeric structure of p300/CBP associated factor.
Bmc Struct.Biol., 14, 2014
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1KAS
 | | BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI | | 分子名称: | BETA-KETOACYL ACP SYNTHASE II | | 著者 | Huang, W, Jia, J, Edwards, P, Dehesh, K, Schneider, G, Lindqvist, Y. | | 登録日 | 1997-12-22 | | 公開日 | 1999-03-02 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (2.4 Å) | | 主引用文献 | Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes.
EMBO J., 17, 1998
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1UBV
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3C0A
 | | Lactobacillus CASEI Thymidylate Synthase Ternary Complex with DUMP and the Phtalimidic Derivative 14C in Multiple Binding Modes-Mode 2 | | 分子名称: | 2'-DEOXYURIDINE 5'-MONOPHOSPHATE, 2-(2-chloropyridin-4-yl)-4-methyl-1H-isoindole-1,3(2H)-dione, Thymidylate synthase | | 著者 | Leone, R, Mangani, S, Cancian, L, Costi, M.P, Luciani, R, Ferrari, S. | | 登録日 | 2008-01-19 | | 公開日 | 2009-01-20 | | 最終更新日 | 2023-11-01 | | 実験手法 | X-RAY DIFFRACTION (2.4 Å) | | 主引用文献 | Identification of the binding modes of N-phenylphthalimides inhibiting bacterial thymidylate synthase through X-ray crystallography screening
J.Med.Chem., 54, 2011
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6C30
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3C26
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1UAE
 | | STRUCTURE OF UDP-N-ACETYLGLUCOSAMINE ENOLPYRUVYL TRANSFERASE | | 分子名称: | UDP-N-ACETYLGLUCOSAMINE ENOLPYRUVYL TRANSFERASE, URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE, [(1R)-1-hydroxypropyl]phosphonic acid | | 著者 | Skarzynski, T. | | 登録日 | 1996-09-30 | | 公開日 | 1997-09-04 | | 最終更新日 | 2024-02-14 | | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | | 主引用文献 | Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin.
Structure, 4, 1996
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1UBX
 | | STRUCTURE OF FARNESYL PYROPHOSPHATE SYNTHETASE | | 分子名称: | FARNESYL DIPHOSPHATE, FARNESYL DIPHOSPHATE SYNTHASE, MAGNESIUM ION | | 著者 | Tarshis, L.C, Proteau, P, Poulter, C.D, Sacchettini, J.C. | | 登録日 | 1996-10-14 | | 公開日 | 1997-03-12 | | 最終更新日 | 2024-02-14 | | 実験手法 | X-RAY DIFFRACTION (2.5 Å) | | 主引用文献 | Regulation of product chain length by isoprenyl diphosphate synthases.
Proc.Natl.Acad.Sci.USA, 93, 1996
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1UBW
 | | STRUCTURE OF FARNESYL PYROPHOSPHATE SYNTHETASE | | 分子名称: | FARNESYL DIPHOSPHATE SYNTHASE, GERANYL DIPHOSPHATE, MAGNESIUM ION | | 著者 | Tarshis, L.C, Proteau, P, Poulter, C.D, Sacchettini, J.C. | | 登録日 | 1996-10-14 | | 公開日 | 1997-03-12 | | 最終更新日 | 2024-02-14 | | 実験手法 | X-RAY DIFFRACTION (2.5 Å) | | 主引用文献 | Regulation of product chain length by isoprenyl diphosphate synthases.
Proc.Natl.Acad.Sci.USA, 93, 1996
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4JH9
 | | Crystal Structure of FosB from Bacillus cereus with Maganese and Potential BSH-Fosfomycin Product | | 分子名称: | (2R)-2-azanyl-3-[(1R,2S)-2-oxidanyl-1-phosphono-propyl]sulfanyl-propanoic acid, MANGANESE (II) ION, Metallothiol transferase FosB | | 著者 | Thompson, M.K, Harp, J, Keithly, M.E, Jagessar, K, Cook, P.D, Armstrong, R.N. | | 登録日 | 2013-03-04 | | 公開日 | 2013-10-02 | | 最終更新日 | 2024-02-28 | | 実験手法 | X-RAY DIFFRACTION (1.77 Å) | | 主引用文献 | Structural and Chemical Aspects of Resistance to the Antibiotic Fosfomycin Conferred by FosB from Bacillus cereus.
Biochemistry, 52, 2013
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1KCE
 | | E. COLI THYMIDYLATE SYNTHASE MUTANT E58Q IN COMPLEX WITH CB3717 AND 2'-DEOXYURIDINE 5'-MONOPHOSPHATE (DUMP) | | 分子名称: | 10-PROPARGYL-5,8-DIDEAZAFOLIC ACID, 2'-DEOXYURIDINE 5'-MONOPHOSPHATE, THYMIDYLATE SYNTHASE | | 著者 | Sage, C.R, Rutenber, E.E, Stout, T.J, Stroud, R.M. | | 登録日 | 1996-10-22 | | 公開日 | 1997-04-21 | | 最終更新日 | 2024-06-05 | | 実験手法 | X-RAY DIFFRACTION (2 Å) | | 主引用文献 | An essential role for water in an enzyme reaction mechanism: the crystal structure of the thymidylate synthase mutant E58Q.
Biochemistry, 35, 1996
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1UBY
 | | STRUCTURE OF FARNESYL PYROPHOSPHATE SYNTHETASE | | 分子名称: | DIMETHYLALLYL DIPHOSPHATE, FARNESYL DIPHOSPHATE SYNTHASE, MAGNESIUM ION | | 著者 | Tarshis, L.C, Proteau, P, Poulter, C.D, Sacchettini, J.C. | | 登録日 | 1996-10-14 | | 公開日 | 1997-03-12 | | 最終更新日 | 2024-02-14 | | 実験手法 | X-RAY DIFFRACTION (2.4 Å) | | 主引用文献 | Regulation of product chain length by isoprenyl diphosphate synthases.
Proc.Natl.Acad.Sci.USA, 93, 1996
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6BJL
 | | Human ABO(H) blood group glycosyltransferase GTB D302L mutant | | 分子名称: | ABO blood group (Transferase A, alpha 1-3-N-acetylgalactosaminyltransferase transferase B, alpha 1-3-galactosyltransferase), ... | | 著者 | Gagnon, S.M.L, Legg, M.S.G, Evans, S.V. | | 登録日 | 2017-11-06 | | 公開日 | 2018-09-19 | | 最終更新日 | 2023-10-04 | | 実験手法 | X-RAY DIFFRACTION (1.69 Å) | | 主引用文献 | Conserved residues Arg188 and Asp302 are critical for active site organization and catalysis in human ABO(H) blood group A and B glycosyltransferases.
Glycobiology, 28, 2018
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5WX4
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4H2O
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