1TIU
 
 | | TITIN, IG REPEAT 27, NMR, 24 STRUCTURES | | Descriptor: | TITIN, I27 | | Authors: | Improta, S, Politou, A.S, Pastore, A. | | Deposit date: | 1996-02-02 | | Release date: | 1996-07-11 | | Last modified: | 2024-05-22 | | Method: | SOLUTION NMR | | Cite: | Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity.
Structure, 4, 1996
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3EXU
 | | A glycoside hydrolase family 11 xylanase with an extended thumb region | | Descriptor: | 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, Endo-1,4-beta-xylanase, GLYCEROL | | Authors: | Vandermarliere, E, Pollet, A, Strelkov, S.V, Delcour, J.A, Courtin, C.M. | | Deposit date: | 2008-10-17 | | Release date: | 2009-08-25 | | Last modified: | 2023-11-01 | | Method: | X-RAY DIFFRACTION (1.81 Å) | | Cite: | Crystallographic and activity-based evidence for thumb flexibility and its relevance in glycoside hydrolase family 11 xylanases
Proteins, 77, 2009
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4AHP
 | | Crystal Structure of Wild Type N-acetylneuraminic acid lyase from Staphylococcus aureus | | Descriptor: | CHLORIDE ION, N-ACETYLNEURAMINATE LYASE | | Authors: | Timms, N, Polyakova, A, Windle, C.L, Trinh, C.H, Nelson, A, Trinh, A.R, Berry, A. | | Deposit date: | 2012-02-06 | | Release date: | 2013-01-23 | | Last modified: | 2023-12-20 | | Method: | X-RAY DIFFRACTION (2.1 Å) | | Cite: | Structural Insights Into the Recovery of Aldolase Activity in N-Acetylneuraminic Acid Lyase by Replacement of the Catalytically Active Lysine with Gamma-Thialysine by Using a Chemical Mutagenesis Strategy.
Chembiochem, 14, 2013
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4AHQ
 | | Crystal Structure of N-acetylneuraminic acid lyase mutant K165C from Staphylococcus aureus | | Descriptor: | N-ACETYLNEURAMINATE LYASE | | Authors: | Timms, N, Polyakova, A, Windle, C.L, Trinh, C.H, Nelson, A, Trinh, A.R, Berry, A. | | Deposit date: | 2012-02-06 | | Release date: | 2013-01-23 | | Last modified: | 2024-05-08 | | Method: | X-RAY DIFFRACTION (1.95 Å) | | Cite: | Structural Insights Into the Recovery of Aldolase Activity in N-Acetylneuraminic Acid Lyase by Replacement of the Catalytically Active Lysine with Gamma-Thialysine by Using a Chemical Mutagenesis Strategy.
Chembiochem, 14, 2013
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4AHO
 | | Crystal Structure of N-acetylneuraminic acid lyase from Staphylococcus aureus with the chemical modification thia-lysine at position 165 | | Descriptor: | CHLORIDE ION, N-ACETYLNEURAMINATE LYASE | | Authors: | Timms, N, Polyakova, A, Windle, C.L, Trinh, C.H, Nelson, A, Trinh, A.R, Berry, A. | | Deposit date: | 2012-02-06 | | Release date: | 2013-01-23 | | Last modified: | 2013-03-13 | | Method: | X-RAY DIFFRACTION (2 Å) | | Cite: | Structural Insights Into the Recovery of Aldolase Activity in N-Acetylneuraminic Acid Lyase by Replacement of the Catalytically Active Lysine with Gamma-Thialysine by Using a Chemical Mutagenesis Strategy.
Chembiochem, 14, 2013
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4AMA
 | | Crystal Structure of N-acetylneuraminic acid lyase from Staphylococcus aureus with the chemical modification thia-lysine at position 165 in complex with pyruvate | | Descriptor: | N-ACETYLNEURAMINATE LYASE | | Authors: | Timms, N, Polyakova, A, Windle, C.L, Trinh, C.H, Nelson, A, Pearson, A.R, Berry, A. | | Deposit date: | 2012-03-08 | | Release date: | 2013-01-23 | | Last modified: | 2019-07-10 | | Method: | X-RAY DIFFRACTION (2.35 Å) | | Cite: | Structural insights into the recovery of aldolase activity in N-acetylneuraminic acid lyase by replacement of the catalytically active lysine with gamma-thialysine by using a chemical mutagenesis strategy.
Chembiochem, 14, 2013
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4B54
 | | The Structure of the inactive mutant G153R of LptC from E. coli | | Descriptor: | ACETATE ION, LIPOPOLYSACCHARIDE EXPORT SYSTEM PROTEIN LPTC | | Authors: | Villa, R, Martorana, A.M, Sperandeo, P, Kahne, D, Okuda, S, Gourlay, L.J, Nardini, M, Bolognesi, M, Polissi, A. | | Deposit date: | 2012-08-02 | | Release date: | 2013-01-16 | | Last modified: | 2023-12-20 | | Method: | X-RAY DIFFRACTION (2.8 Å) | | Cite: | The Escherichia Coli Lpt Transenvelope Protein Complex for Lipopolysaccharide Export is Assembled Via Conserved Structurally Homologous Domains.
J.Bacteriol., 195, 2013
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