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PDB: 241 件

1XYC
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X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE ISOMERASE-SUBSTRATE COMPLEXES POSITION THE SUBSTRATE AND PROVIDE EVIDENCE FOR METAL MOVEMENT DURING CATALYSIS
分子名称: 3-O-METHYLFRUCTOSE IN LINEAR FORM, MAGNESIUM ION, XYLOSE ISOMERASE
著者Lavie, A, Allen, K.N, Petsko, G.A, Ringe, D.
登録日1994-01-03
公開日1994-05-31
最終更新日2024-02-14
実験手法X-RAY DIFFRACTION (2.19 Å)
主引用文献X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis.
Biochemistry, 33, 1994
1XYB
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X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE ISOMERASE-SUBSTRATE COMPLEXES POSITION THE SUBSTRATE AND PROVIDE EVIDENCE FOR METAL MOVEMENT DURING CATALYSIS
分子名称: D-glucose, MAGNESIUM ION, XYLOSE ISOMERASE
著者Lavie, A, Allen, K.N, Petsko, G.A, Ringe, D.
登録日1994-01-03
公開日1994-05-31
最終更新日2024-02-14
実験手法X-RAY DIFFRACTION (1.96 Å)
主引用文献X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis.
Biochemistry, 33, 1994
1ASA
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THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE Y226F(Y225F) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE
分子名称: ASPARTATE AMINOTRANSFERASE, MALEIC ACID, PYRIDOXAL-5'-PHOSPHATE
著者Schumacher, C, Ringe, D.
登録日1993-08-27
公開日1994-04-30
最終更新日2024-06-05
実験手法X-RAY DIFFRACTION (2.4 Å)
主引用文献The Structural Basis for the Reduced Activity of the Y226F(Y225F) Active Site Mutant of E. Coli Aspartate Aminotransferase
To be Published
1ELE
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STRUCTURAL ANALYSIS OF THE ACTIVE SITE OF PORCINE PANCREATIC ELASTASE BASED ON THE X-RAY CRYSTAL STRUCTURES OF COMPLEXES WITH TRIFLUOROACETYL-DIPEPTIDE-ANILIDE INHIBITORS
分子名称: CALCIUM ION, ELASTASE, N-(trifluoroacetyl)-L-valyl-N-[4-(trifluoromethyl)phenyl]-L-alaninamide, ...
著者Mattos, C, Petsko, G.A, Ringe, D.
登録日1994-10-24
公開日1995-02-14
最終更新日2024-06-05
実験手法X-RAY DIFFRACTION (2 Å)
主引用文献Structural analysis of the active site of porcine pancreatic elastase based on the X-ray crystal structures of complexes with trifluoroacetyl-dipeptide-anilide inhibitors.
Biochemistry, 34, 1995
1ELD
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Structural analysis of the active site of porcine pancreatic elastase based on the x-ray crystal structures of complexes with trifluoroacetyl-dipeptide-anilide inhibitors
分子名称: ACETIC ACID, CALCIUM ION, ELASTASE, ...
著者Mattos, C, Petsko, G.A, Ringe, D.
登録日1994-10-24
公開日1995-02-14
最終更新日2024-06-05
実験手法X-RAY DIFFRACTION (2 Å)
主引用文献Structural analysis of the active site of porcine pancreatic elastase based on the X-ray crystal structures of complexes with trifluoroacetyl-dipeptide-anilide inhibitors.
Biochemistry, 34, 1995
6RHN
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BU of 6rhn by Molmil
HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT WITHOUT NUCLEOTIDE
分子名称: HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN
著者Brenner, C, Garrison, P, Gilmour, J, Peisach, D, Ringe, D, Petsko, G.A, Lowenstein, J.M.
登録日1997-02-27
公開日1997-06-16
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (2.15 Å)
主引用文献Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins.
Nat.Struct.Biol., 4, 1997
3DHC
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1.3 Angstrom Structure of N-Acyl Homoserine Lactone Hydrolase with the Product N-Hexanoyl-L-Homocysteine Bound to The catalytic Metal Center
分子名称: GLYCEROL, N-Acyl Homoserine Lactone Hydrolase, N-hexanoyl-L-homocysteine, ...
著者Liu, D, Momb, J, Thomas, P.W, Moulin, A, Petsko, G.A, Fast, W, Ringe, D.
登録日2008-06-17
公開日2008-07-29
最終更新日2023-08-30
実験手法X-RAY DIFFRACTION (1.3 Å)
主引用文献Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures.
Biochemistry, 47, 2008
3DHA
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An Ultral High Resolution Structure of N-Acyl Homoserine Lactone Hydrolase with the Product N-Hexanoyl-L-Homoserine Bound at An Alternative Site
分子名称: GLYCEROL, N-Acyl Homoserine Lactone Hydrolase, N-hexanoyl-L-homoserine, ...
著者Liu, D, Momb, J, Thomas, P.W, Moulin, A, Petsko, G.A, Fast, W, Ringe, D.
登録日2008-06-17
公開日2008-07-29
最終更新日2023-08-30
実験手法X-RAY DIFFRACTION (0.95 Å)
主引用文献Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures.
Biochemistry, 47, 2008
3DHB
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1.4 Angstrom Structure of N-Acyl Homoserine Lactone Hydrolase with the Product N-Hexanoyl-L-Homoserine Bound at The Catalytic Metal Center
分子名称: GLYCEROL, N-Acyl Homoserine Lactone Hydrolase, N-hexanoyl-L-homoserine, ...
著者Liu, D, Momb, J, Thomas, P.W, Moulin, A, Petsko, G.A, Fast, W, Ringe, D.
登録日2008-06-17
公開日2008-07-29
最終更新日2023-08-30
実験手法X-RAY DIFFRACTION (1.4 Å)
主引用文献Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures.
Biochemistry, 47, 2008
1A0G
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L201A MUTANT OF D-AMINO ACID AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAMINE-5'-PHOSPHATE
分子名称: 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE, D-AMINO ACID AMINOTRANSFERASE
著者Sugio, S, Kashima, A, Kishimoto, K, Peisach, D, Petsko, G.A, Ringe, D, Yoshimura, T, Esaki, N.
登録日1997-11-30
公開日1998-06-03
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (2 Å)
主引用文献Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0 A resolution: implication of the structural role of Leu201 in transamination.
Protein Eng., 11, 1998
1TPC
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BU of 1tpc by Molmil
OFFSET OF A CATALYTIC LESION BY A BOUND WATER SOLUBLE
分子名称: PHOSPHOGLYCOLOHYDROXAMIC ACID, TRIOSEPHOSPHATE ISOMERASE
著者Zhang, Z, Sugio, S, Komives, E.A, Liu, K.D, Knowles, J.R, Petsko, G.A, Ringe, D.
登録日1994-02-03
公開日1995-02-14
最終更新日2024-02-14
実験手法X-RAY DIFFRACTION (1.9 Å)
主引用文献The structural basis for pseudoreversion of the E165D lesion by the secondary S96P mutation in triosephosphate isomerase depends on the positions of active site water molecules.
Biochemistry, 34, 1995
5T4J
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PLP and GABA Trigger GabR-Mediated Transcription Regulation in Bacillus subsidies via External Aldimine Formation
分子名称: GAMMA-AMINO-BUTANOIC ACID, HTH-type transcriptional regulatory protein GabR, PYRIDOXAL-5'-PHOSPHATE
著者Wu, R, Sanishvili, R, Belitsky, B.R, Juncosa, J.I, Le, H.V, Lehrer, H.J.S, Farley, M, Silverman, R.B, Petsko, G.A, Ringe, D, Liu, D.
登録日2016-08-29
公開日2017-03-29
最終更新日2023-11-15
実験手法X-RAY DIFFRACTION (2.231 Å)
主引用文献PLP and GABA trigger GabR-mediated transcription regulation in Bacillus subtilis via external aldimine formation.
Proc. Natl. Acad. Sci. U.S.A., 114, 2017
5T4L
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PLP and GABA Trigger GabR-Mediated Transcription Regulation in Bacillus subsidies via External Aldimine Formation
分子名称: (4R)-4-amino-6-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}hexanoic acid, Aspartate aminotransferase
著者Wu, R, Sanishvili, R, Belitsky, B.R, Juncosa, J.I, Le, H.V, Lehrer, H.J.S, Farley, M, Silverman, R.B, Petsko, G.A, Ringe, D, Liu, D.
登録日2016-08-29
公開日2017-03-29
最終更新日2023-10-04
実験手法X-RAY DIFFRACTION (1.53 Å)
主引用文献PLP and GABA trigger GabR-mediated transcription regulation in Bacillus subtilis via external aldimine formation.
Proc. Natl. Acad. Sci. U.S.A., 114, 2017
5T4K
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BU of 5t4k by Molmil
PLP and GABA Trigger GabR-Mediated Transcription Regulation in Bacillus subsidies via External Aldimine Formation
分子名称: (4S)-5-fluoro-4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]pentanoic acid, HTH-type transcriptional regulatory protein GabR
著者Wu, R, Sanishvili, R, Belitsky, B.R, Juncosa, J.I, Le, H.V, Lehrer, H.J.S, Farley, M, Silverman, R.B, Petsko, G.A, Ringe, D, Liu, D.
登録日2016-08-29
公開日2017-03-29
最終更新日2023-10-04
実験手法X-RAY DIFFRACTION (2.245 Å)
主引用文献PLP and GABA trigger GabR-mediated transcription regulation in Bacillus subtilis via external aldimine formation.
Proc. Natl. Acad. Sci. U.S.A., 114, 2017
4DAA
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BU of 4daa by Molmil
CRYSTALLOGRAPHIC STRUCTURE OF D-AMINO ACID AMINOTRANSFERASE IN PYRIDOXAL-5'-PHOSPHATE (PLP) FORM
分子名称: D-AMINO ACID AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE, SULFATE ION
著者Peisach, D, Chipman, D.M, Ringe, D.
登録日1998-01-26
公開日1998-04-29
最終更新日2023-08-09
実験手法X-RAY DIFFRACTION (2.4 Å)
主引用文献Crystallographic study of steps along the reaction pathway of D-amino acid aminotransferase.
Biochemistry, 37, 1998
5UCD
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BU of 5ucd by Molmil
Benzaldehyde Dehydrogenase, a Class 3 Aldehyde Dehydrogenase, with bound NADP+ and Benzoate Adduct
分子名称: NAD(P)-dependent benzaldehyde dehydrogenase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
著者Zahniser, M.P.D, Prasad, S, Kneen, M.M, Kreinbring, C.A, Petsko, G.A, Ringe, D, McLeish, M.J.
登録日2016-12-22
公開日2017-04-12
最終更新日2023-10-04
実験手法X-RAY DIFFRACTION (2.28 Å)
主引用文献Structure and mechanism of benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633, a member of the Class 3 aldehyde dehydrogenase superfamily.
Protein Eng. Des. Sel., 30, 2017
1ASG
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BU of 1asg by Molmil
THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE Y226F(Y225F) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE
分子名称: ASPARTATE AMINOTRANSFERASE, MALEIC ACID, PYRIDOXAL-5'-PHOSPHATE
著者Schumacher, C, Ringe, D.
登録日1993-08-27
公開日1994-04-30
最終更新日2024-06-05
実験手法X-RAY DIFFRACTION (2.8 Å)
主引用文献The Structural Basis for the Reduced Activity of the Y226F(Y225F) Active Site Mutant of E. Coli Aspartate Aminotransferase
To be Published
1ASE
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THE STRUCTURE OF WILD TYPE E. COLI ASPARTATE AMINOTRANSFERASE RECONSTITUTED WITH PLP-N-OXIDE
分子名称: ASPARTATE AMINOTRANSFERASE, MALEIC ACID, PYRIDOXAL-5'-PHOSPHATE-N-OXIDE
著者Schumacher, C, Ringe, D.
登録日1993-08-27
公開日1994-04-30
最終更新日2024-06-05
実験手法X-RAY DIFFRACTION (2.5 Å)
主引用文献The Structure of Wild Type E. Coli Aspartate Aminotransferase Reconstituted with Plp-N-Oxide
To be Published
1ASB
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THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE D223A(D222A) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE
分子名称: ASPARTATE AMINOTRANSFERASE, MALEIC ACID, PYRIDOXAL-5'-PHOSPHATE
著者Schumacher, C, Ringe, D.
登録日1993-08-27
公開日1994-04-30
最終更新日2024-06-05
実験手法X-RAY DIFFRACTION (2.6 Å)
主引用文献The Structural Basis for the Reduced Activity of the D223A(D222A) Active Site Mutant of E. Coli Aspartate Aminotransferase
To be Published
1ASD
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THE STRUCTURE OF WILD TYPE E. COLI ASPARTATE AMINOTRANSFERASE RECONSTITUTED WITH N-MEPLP
分子名称: ASPARTATE AMINOTRANSFERASE, MALEIC ACID, N-METHYL-PYRIDOXAL-5'-PHOSPHATE
著者Schumacher, C, Ringe, D.
登録日1993-08-27
公開日1994-04-30
最終更新日2024-06-05
実験手法X-RAY DIFFRACTION (2.2 Å)
主引用文献The Structure of Wild Type E. Coli Aspartate Aminotransferase Reconstituted with N-Meplp
To be Published
5UGQ
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Crystal Structure of Hip1 (Rv2224c)
分子名称: Carboxylesterase A
著者Naffin-Olivos, J.L, Daab, A, White, A, Goldfarb, N, Milne, A.C, Liu, D, Dunn, B.M, Rengarajan, J, Petsko, G.A, Ringe, D.
登録日2017-01-09
公開日2017-04-12
最終更新日2019-12-11
実験手法X-RAY DIFFRACTION (2.609 Å)
主引用文献Structure Determination of Mycobacterium tuberculosis Serine Protease Hip1 (Rv2224c).
Biochemistry, 56, 2017
2SFP
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ALANINE RACEMASE WITH BOUND PROPIONATE INHIBITOR
分子名称: PROPANOIC ACID, PROTEIN (ALANINE RACEMASE), PYRIDOXAL-5'-PHOSPHATE
著者Morollo, A.A, Petsko, G.A, Ringe, D.
登録日1999-02-16
公開日1999-02-24
最終更新日2023-11-15
実験手法X-RAY DIFFRACTION (1.9 Å)
主引用文献Structure of a Michaelis complex analogue: propionate binds in the substrate carboxylate site of alanine racemase.
Biochemistry, 38, 1999
5UOH
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BU of 5uoh by Molmil
Crystal Structure of Hip1 (Rv2224c) T466A mutant
分子名称: Carboxylesterase A
著者Naffin-Olivos, J.L, Daab, A, White, A, Goldfarb, N, Milne, A.C, Liu, D, Baikovitz, J, Dunn, B.M, Rengarajan, J, Petsko, G.A, Ringe, D.
登録日2017-01-31
公開日2017-04-12
最終更新日2019-12-11
実験手法X-RAY DIFFRACTION (2.609 Å)
主引用文献Structure Determination of Mycobacterium tuberculosis Serine Protease Hip1 (Rv2224c).
Biochemistry, 56, 2017
5UNO
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BU of 5uno by Molmil
Crystal Structure of Hip1 (Rv2224c)
分子名称: Carboxylesterase A
著者Naffin-Olivos, J.L, Daab, A, White, A, Goldfarb, N, Milne, A.C, Liu, D, Dunn, B.M, Rengarajan, J, Petsko, G.A, Ringe, D.
登録日2017-01-31
公開日2017-04-12
最終更新日2019-12-11
実験手法X-RAY DIFFRACTION (2.603 Å)
主引用文献Structure Determination of Mycobacterium tuberculosis Serine Protease Hip1 (Rv2224c).
Biochemistry, 56, 2017
5VWQ
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E.coli Aspartate aminotransferase-(1R,3S,4S)-3-amino-4-fluorocyclopentane-1-carboxylic acid (FCP)
分子名称: 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE, Aspartate aminotransferase
著者Mascarenhas, R, Lehrer, H, Liu, D, Ringe, D.
登録日2017-05-22
公開日2017-08-30
最終更新日2023-11-29
実験手法X-RAY DIFFRACTION (1.8 Å)
主引用文献Selective Targeting by a Mechanism-Based Inactivator against Pyridoxal 5'-Phosphate-Dependent Enzymes: Mechanisms of Inactivation and Alternative Turnover.
Biochemistry, 56, 2017

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