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5L09
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BU of 5l09 by Molmil
Crystal Structure of Quorum-Sensing Transcriptional Activator from Yersinia enterocolitica in complex with 3-oxo-N-[(3S)-2-oxotetrahydrofuran-3-yl]hexanamide
分子名称: 1,2-ETHANEDIOL, 3-oxo-N-[(3S)-2-oxotetrahydrofuran-3-yl]hexanamide, ACETIC ACID, ...
著者Kim, Y, Chhor, G, Jedrzejczak, R, Winans, S.C, Anderson, W.F, Joachimiak, A, Center for Structural Genomics of Infectious Diseases (CSGID)
登録日2016-07-26
公開日2016-09-07
最終更新日2023-11-15
実験手法X-RAY DIFFRACTION (2 Å)
主引用文献Crystal Structure of Quorum-Sensing Transcriptional Activator from Yersinia enterocolitica
To Be Published
5K9A
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BU of 5k9a by Molmil
Sortase A from Corynebacterium diphtheriae
分子名称: Putative fimbrial associated sortase-like protein, SULFATE ION
著者Osipiuk, J, Huang, I.-H, Ma, X, Ton-That, H, Anderson, W.F, Joachimiak, A, Center for Structural Genomics of Infectious Diseases (CSGID)
登録日2016-05-31
公開日2016-06-15
最終更新日2023-09-27
実験手法X-RAY DIFFRACTION (2.1 Å)
主引用文献In vitro reconstitution of sortase-catalyzed pilus polymerization reveals structural elements involved in pilin cross-linking.
Proc.Natl.Acad.Sci.USA, 115, 2018
3N3T
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BU of 3n3t by Molmil
Crystal structure of putative diguanylate cyclase/phosphodiesterase complex with cyclic di-gmp
分子名称: 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one), CHLORIDE ION, MAGNESIUM ION, ...
著者Chang, C, Xu, X, Cui, H, Savchenko, A, Edwards, A, Joachimiak, A, Midwest Center for Structural Genomics (MCSG)
登録日2010-05-20
公開日2010-06-16
最終更新日2017-11-08
実験手法X-RAY DIFFRACTION (2.35 Å)
主引用文献Structural insight into the mechanism of c-di-GMP hydrolysis by EAL domain phosphodiesterases.
J.Mol.Biol., 402, 2010
3KKW
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BU of 3kkw by Molmil
Crystal structure of His-tagged form of PA4794 protein
分子名称: 1,2-ETHANEDIOL, Putative uncharacterized protein, SULFATE ION
著者Majorek, K.A, Chruszcz, M, Joachimiak, A, Minor, W, Midwest Center for Structural Genomics (MCSG)
登録日2009-11-06
公開日2009-11-24
最終更新日2023-09-06
実験手法X-RAY DIFFRACTION (1.41 Å)
主引用文献Double trouble-Buffer selection and His-tag presence may be responsible for nonreproducibility of biomedical experiments.
Protein Sci., 23, 2014
1L34
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BU of 1l34 by Molmil
HIGH-RESOLUTION STRUCTURE OF THE TEMPERATURE-SENSITIVE MUTANT OF PHAGE LYSOZYME, ARG 96 (RIGHT ARROW) HIS
分子名称: T4 LYSOZYME
著者Weaver, L.H, Matthews, B.W.
登録日1989-05-01
公開日1990-01-15
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.9 Å)
主引用文献High-resolution structure of the temperature-sensitive mutant of phage lysozyme, Arg 96----His.
Biochemistry, 28, 1989
1L21
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BU of 1l21 by Molmil
CONTRIBUTIONS OF LEFT-HANDED HELICAL RESIDUES TO THE STRUCTURE AND STABILITY OF BACTERIOPHAGE T4 LYSOZYME
分子名称: T4 LYSOZYME
著者Nicholson, H, Matthews, B.W.
登録日1989-05-01
公開日1990-01-15
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.85 Å)
主引用文献Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme.
J.Mol.Biol., 210, 1989
1L28
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BU of 1l28 by Molmil
REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY
分子名称: T4 LYSOZYME
著者Bell, J.A, Dao-Pin, S, Matthews, B.W.
登録日1989-05-01
公開日1990-01-15
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.9 Å)
主引用文献Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability.
Science, 239, 1988
1L33
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BU of 1l33 by Molmil
CONTRIBUTIONS OF LEFT-HANDED HELICAL RESIDUES TO THE STRUCTURE AND STABILITY OF BACTERIOPHAGE T4 LYSOZYME
分子名称: T4 LYSOZYME
著者Nicholson, H, Matthews, B.W.
登録日1989-05-01
公開日1990-01-15
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.7 Å)
主引用文献Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme.
J.Mol.Biol., 210, 1989
1L17
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BU of 1l17 by Molmil
HYDROPHOBIC STABILIZATION IN T4 LYSOZYME DETERMINED DIRECTLY BY MULTIPLE SUBSTITUTIONS OF ILE 3
分子名称: T4 LYSOZYME
著者Matsumura, M, Dao-Pin, S, Matthews, B.W.
登録日1989-05-01
公開日1990-01-15
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.7 Å)
主引用文献Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3.
Nature, 334, 1988
1L24
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BU of 1l24 by Molmil
ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING
分子名称: T4 LYSOZYME
著者Nicholson, H, Matthews, B.W.
登録日1989-05-01
公開日1990-01-15
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.7 Å)
主引用文献Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding.
Proc.Natl.Acad.Sci.USA, 84, 1987
1L18
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BU of 1l18 by Molmil
HYDROPHOBIC STABILIZATION IN T4 LYSOZYME DETERMINED DIRECTLY BY MULTIPLE SUBSTITUTIONS OF ILE 3
分子名称: T4 LYSOZYME
著者Matsumura, M, Dao-Pin, S, Matthews, B.W.
登録日1989-05-01
公開日1990-01-15
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.7 Å)
主引用文献Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3.
Nature, 334, 1988
1L32
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BU of 1l32 by Molmil
REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY
分子名称: T4 LYSOZYME
著者Bell, J.A, Dao-Pin, S, Matthews, B.W.
登録日1989-05-01
公開日1990-01-15
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.7 Å)
主引用文献Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability.
Science, 239, 1988
1L27
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BU of 1l27 by Molmil
REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY
分子名称: T4 LYSOZYME
著者Bell, J.A, Dao-Pin, S, Matthews, B.W.
登録日1989-05-01
公開日1990-01-15
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.8 Å)
主引用文献Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability.
Science, 239, 1988
1L30
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BU of 1l30 by Molmil
REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY
分子名称: T4 LYSOZYME
著者Bell, J.A, Dao-Pin, S, Matthews, B.W.
登録日1989-05-01
公開日1990-01-15
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.7 Å)
主引用文献Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability.
Science, 239, 1988
1L25
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BU of 1l25 by Molmil
REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY
分子名称: T4 LYSOZYME
著者Bell, J.A, Dao-Pin, S, Matthews, B.W.
登録日1989-05-01
公開日1990-01-15
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.8 Å)
主引用文献Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability.
Science, 239, 1988
1L31
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BU of 1l31 by Molmil
REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY
分子名称: T4 LYSOZYME
著者Bell, J.A, Dao-Pin, S, Matthews, B.W.
登録日1989-05-01
公開日1990-01-15
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.8 Å)
主引用文献Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability.
Science, 239, 1988
1L35
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BU of 1l35 by Molmil
STRUCTURE OF A THERMOSTABLE DISULFIDE-BRIDGE MUTANT OF PHAGE T4 LYSOZYME SHOWS THAT AN ENGINEERED CROSSLINK IN A FLEXIBLE REGION DOES NOT INCREASE THE RIGIDITY OF THE FOLDED PROTEIN
分子名称: T4 LYSOZYME
著者Pjura, P.E, Matsumura, M, Wozniak, J.A, Matthews, B.W.
登録日1989-10-26
公開日1990-01-15
最終更新日2022-11-23
実験手法X-RAY DIFFRACTION (1.8 Å)
主引用文献Structure of a thermostable disulfide-bridge mutant of phage T4 lysozyme shows that an engineered cross-link in a flexible region does not increase the rigidity of the folded protein.
Biochemistry, 29, 1990
1L19
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BU of 1l19 by Molmil
ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES
分子名称: T4 LYSOZYME
著者Nicholson, H, Matthews, B.W.
登録日1989-05-01
公開日1990-01-15
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.7 Å)
主引用文献Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles.
Nature, 336, 1988
1L22
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BU of 1l22 by Molmil
CONTRIBUTIONS OF LEFT-HANDED HELICAL RESIDUES TO THE STRUCTURE AND STABILITY OF BACTERIOPHAGE T4 LYSOZYME
分子名称: T4 LYSOZYME
著者Nicholson, H, Matthews, B.W.
登録日1989-05-01
公開日1990-01-15
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.7 Å)
主引用文献Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme.
J.Mol.Biol., 210, 1989
1L23
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BU of 1l23 by Molmil
ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING
分子名称: T4 LYSOZYME
著者Nicholson, H, Matthews, B.W.
登録日1989-05-01
公開日1990-01-15
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.7 Å)
主引用文献Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding.
Proc.Natl.Acad.Sci.USA, 84, 1987
1L20
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BU of 1l20 by Molmil
ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES
分子名称: T4 LYSOZYME
著者Nicholson, H, Matthews, B.W.
登録日1989-05-01
公開日1990-01-15
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.85 Å)
主引用文献Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles.
Nature, 336, 1988
1L29
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BU of 1l29 by Molmil
REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY
分子名称: T4 LYSOZYME
著者Bell, J.A, Dao-Pin, S, Matthews, B.W.
登録日1989-05-01
公開日1990-01-15
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.7 Å)
主引用文献Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability.
Science, 239, 1988
1L26
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BU of 1l26 by Molmil
REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY
分子名称: BETA-MERCAPTOETHANOL, T4 LYSOZYME
著者Bell, J.A, Dao-Pin, S, Matthews, B.W.
登録日1989-05-01
公開日1990-01-15
最終更新日2022-11-23
実験手法X-RAY DIFFRACTION (1.7 Å)
主引用文献Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability.
Science, 239, 1988
4L8A
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BU of 4l8a by Molmil
Crystal structure of a GNAT superfamily acetyltransferase PA4794 in ternary complex with N-Phenylacetyl-Gly-AcLys and CoA
分子名称: 1,2-ETHANEDIOL, COENZYME A, N-(phenylacetyl)glycyl-N~6~-acetyl-L-lysine, ...
著者Majorek, K.A, Chruszcz, M, Joachimiak, A, Minor, W, Midwest Center for Structural Genomics (MCSG)
登録日2013-06-16
公開日2013-07-10
最終更新日2023-11-29
実験手法X-RAY DIFFRACTION (1.2 Å)
主引用文献Structural, functional, and inhibition studies of a Gcn5-related N-acetyltransferase (GNAT) superfamily protein PA4794: a new C-terminal lysine protein acetyltransferase from pseudomonas aeruginosa.
J.Biol.Chem., 288, 2013
4KOS
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BU of 4kos by Molmil
Crystal structure of a GNAT superfamily acetyltransferase PA4794 in complex with Cefmetazole
分子名称: (6R,7S)-7-({[(cyanomethyl)sulfanyl]acetyl}amino)-7-methoxy-3-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-8-oxo-5-thia -1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, 1,2-ETHANEDIOL, SULFATE ION, ...
著者Majorek, K.A, Chruszcz, M, Joachimiak, A, Minor, W, Midwest Center for Structural Genomics (MCSG)
登録日2013-05-12
公開日2013-06-05
最終更新日2023-09-20
実験手法X-RAY DIFFRACTION (1.55 Å)
主引用文献Structural, Functional, and Inhibition Studies of a Gcn5-related N-Acetyltransferase (GNAT) Superfamily Protein PA4794: A NEW C-TERMINAL LYSINE PROTEIN ACETYLTRANSFERASE FROM PSEUDOMONAS AERUGINOSA.
J.Biol.Chem., 288, 2013

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