1ZQZ
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1ZQG
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1ZQS
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1ZQP
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1ZQO
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1ZQR
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1ZQB
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1ZQJ
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1ZQY
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1ZQF
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1ZQM
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1ZQX
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1ZQA
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1ZQK
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1ZQV
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1ZQE
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1ZQQ
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1MKT
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6B4M
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![BU of 6b4m by Molmil](/molmil-images/mine/6b4m) | Structural characterization of a novel monotreme-specific protein from the milk of the platypus | Descriptor: | 2-acetamido-2-deoxy-beta-D-glucopyranose, GLYCEROL, IODIDE ION, ... | Authors: | Peat, T.S, Newman, J, Sharp, J.A, Kumar, A, Nicholas, K.R, Adams, T.E. | Deposit date: | 2017-09-27 | Release date: | 2018-01-17 | Last modified: | 2023-10-04 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Structural characterization of a novel monotreme-specific protein with antimicrobial activity from the milk of the platypus. Acta Crystallogr F Struct Biol Commun, 74, 2018
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2MAU
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3SDZ
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![BU of 3sdz by Molmil](/molmil-images/mine/3sdz) | Structural characterization of the subunit A mutant F427W of the A-ATP synthase from Pyrococcus horikoshii | Descriptor: | (4S)-2-METHYL-2,4-PENTANEDIOL, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ACETIC ACID, ... | Authors: | Tadwal, V.S, Manimekalai, M.S.S, Balakrishna, A.M, Gruber, G. | Deposit date: | 2011-06-09 | Release date: | 2012-01-25 | Last modified: | 2023-11-01 | Method: | X-RAY DIFFRACTION (2.53 Å) | Cite: | Engineered tryptophan in the adenine-binding pocket of catalytic subunit A of A-ATP synthase demonstrates the importance of aromatic residues in adenine binding, forming a tool for steady-state and time-resolved fluorescence spectroscopy. Acta Crystallogr.,Sect.F, 67, 2011
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3SE0
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![BU of 3se0 by Molmil](/molmil-images/mine/3se0) | Structural characterization of the subunit A mutant F508W of the A-ATP synthase from Pyrococcus horikoshii | Descriptor: | (4S)-2-METHYL-2,4-PENTANEDIOL, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ACETIC ACID, ... | Authors: | Tadwal, V.S, Manimekalai, M.S.S, Balakrishna, A.M, Gruber, G. | Deposit date: | 2011-06-09 | Release date: | 2012-01-25 | Last modified: | 2023-11-01 | Method: | X-RAY DIFFRACTION (2.62 Å) | Cite: | Engineered tryptophan in the adenine-binding pocket of catalytic subunit A of A-ATP synthase demonstrates the importance of aromatic residues in adenine binding, forming a tool for steady-state and time-resolved fluorescence spectroscopy. Acta Crystallogr.,Sect.F, 67, 2011
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2NAF
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![BU of 2naf by Molmil](/molmil-images/mine/2naf) | Solution structure of peptidyl-tRNA hydrolase from Mycobacterium smegmatis | Descriptor: | Peptidyl-tRNA hydrolase | Authors: | Yadav, R, Pathak, P, Fatma, F, Kabra, A, Pulavarti, S, Jain, A, Kumar, A, Shukla, V, Arora, A. | Deposit date: | 2015-12-23 | Release date: | 2017-01-11 | Last modified: | 2024-05-15 | Method: | SOLUTION NMR | Cite: | Structural characterization of peptidyl-tRNA hydrolase from Mycobacterium smegmatis by NMR spectroscopy. Biochim.Biophys.Acta, 1864, 2016
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6A8M
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![BU of 6a8m by Molmil](/molmil-images/mine/6a8m) | N-terminal domain of FACT complex subunit SPT16 from Eremothecium gossypii (Ashbya gossypii) | Descriptor: | FACT complex subunit SPT16 | Authors: | Gaur, N.K, Are, V.N, Durani, V, Ghosh, B, Kumar, A, Kulkarni, K, Makde, R.D. | Deposit date: | 2018-07-09 | Release date: | 2018-08-15 | Last modified: | 2023-11-22 | Method: | X-RAY DIFFRACTION (1.7 Å) | Cite: | Evolutionary conservation of protein dynamics: insights from all-atom molecular dynamics simulations of 'peptidase' domain of Spt16. J.Biomol.Struct.Dyn., 2021
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227D
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![BU of 227d by Molmil](/molmil-images/mine/227d) | A CRYSTALLOGRAPHIC AND SPECTROSCOPIC STUDY OF THE COMPLEX BETWEEN D(CGCGAATTCGCG)2 AND 2,5-BIS(4-GUANYLPHENYL)FURAN, AN ANALOGUE OF BERENIL. STRUCTURAL ORIGINS OF ENHANCED DNA-BINDING AFFINITY | Descriptor: | 2,5-BIS(4-GUANYLPHENYL)FURAN, DNA (5'-D(*CP*GP*CP*GP*AP*AP*TP*TP*CP*GP*CP*G)-3') | Authors: | Laughton, C.A, Tanious, F, Nunn, C.M, Boykin, D.W, Wilson, W.D, Neidle, S. | Deposit date: | 1995-08-08 | Release date: | 1995-11-11 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | A crystallographic and spectroscopic study of the complex between d(CGCGAATTCGCG)2 and 2,5-bis(4-guanylphenyl)furan, an analogue of berenil. Structural origins of enhanced DNA-binding affinity. Biochemistry, 35, 1996
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