4AFT
| Aplysia californica AChBP in complex with Varenicline | Descriptor: | SOLUBLE ACETYLCHOLINE RECEPTOR, VARENICLINE | Authors: | Rucktooa, P, Haseler, C.A, vanElke, R, Smit, A.B, Gallagher, T, Sixma, T.K. | Deposit date: | 2012-01-23 | Release date: | 2012-05-02 | Last modified: | 2023-12-20 | Method: | X-RAY DIFFRACTION (3.2 Å) | Cite: | Structural Characterization of Binding Mode of Smoking Cessation Drugs to Nicotinic Acetylcholine Receptors Through Study of Ligand Complexes with Acetylcholine-Binding Protein. J.Biol.Chem., 287, 2012
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2G8Z
| Crystal structure of the ternary complex of signalling protein from sheep (SPS-40) with trimer and designed peptide at 2.5A resolution | Descriptor: | (TRP)(PRO)(TRP), 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, Chitinase-3-like protein 1, ... | Authors: | Ethayathulla, A.S, Srivastava, D.B, Kumar, J, Somvanshi, R.K, Sharma, S, Singh, T.P. | Deposit date: | 2006-03-04 | Release date: | 2006-04-04 | Last modified: | 2023-10-25 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Crystal structure of the ternary complex of signalling protein from sheep (SPS-40) with trimer and designed peptide at 2.5A resolution To be Published
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4TXY
| Crystal structure of Vibrio cholerae DncV cyclic AMP-GMP synthase, a prokaryotic cGAS homolog | Descriptor: | Cyclic AMP-GMP synthase, MAGNESIUM ION | Authors: | Kranzusch, P.J, Lee, A.S.Y, Wilson, S.C, Solovykh, M.S, Vance, R.E, Berger, J.M, Doudna, J.A. | Deposit date: | 2014-07-07 | Release date: | 2014-08-13 | Last modified: | 2023-12-27 | Method: | X-RAY DIFFRACTION (3.0001 Å) | Cite: | Structure-Guided Reprogramming of Human cGAS Dinucleotide Linkage Specificity. Cell, 158, 2014
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2HPZ
| Crystal structure of proteinase K complex with a synthetic peptide KLKLLVVIRLK at 1.69 A resolution | Descriptor: | 11-mer synthetic peptide, CALCIUM ION, NITRATE ION, ... | Authors: | Prem kumar, R, Singh, A.K, Somvanshi, R.K, Singh, N, Sharma, S, Kaur, P, Dey, S, Bhushan, A, Singh, T.P. | Deposit date: | 2006-07-18 | Release date: | 2006-08-01 | Last modified: | 2023-10-25 | Method: | X-RAY DIFFRACTION (1.69 Å) | Cite: | Crystal structure of proteinase K complex with a synthetic peptide KLKLLVVIRLK at 1.69 A resolution To be Published
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2GNS
| Design of specific peptide inhibitors of phospholipase A2: Crystal structure of the complex formed between a group II phospholipase A2 and a designed pentapeptide Ala- Leu- Val- Tyr- Lys at 2.3 A resolution | Descriptor: | ALVYK, Phospholipase A2 VRV-PL-VIIIa, SULFATE ION | Authors: | Singh, N, Sharma, S, Somvanshi, R.K, Dey, S, Singh, T.P. | Deposit date: | 2006-04-11 | Release date: | 2006-04-25 | Last modified: | 2024-10-09 | Method: | X-RAY DIFFRACTION (2.3 Å) | Cite: | Design of specific peptide inhibitors of phospholipase A2: Crystal structure of the complex formed between a group II phospholipase A2 and a designed pentapeptide Ala - Leu - Val - Tyr - Lys at 2.3 A resolution To be Published
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2LM8
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2MT5
| Isolated Ring domain | Descriptor: | Anaphase-promoting complex subunit 11, ZINC ION | Authors: | Brown, N.G, Watson, E.R, Weissman, F, Royappa, G, Schulman, B, Jarvis, M, Vanderlinden, R, Frye, J.J, Qiao, R, Petzold, G, Peters, J, Stark, H. | Deposit date: | 2014-08-13 | Release date: | 2014-10-29 | Last modified: | 2024-05-15 | Method: | SOLUTION NMR | Cite: | Mechanism of Polyubiquitination by Human Anaphase-Promoting Complex: RING Repurposing for Ubiquitin Chain Assembly. Mol.Cell, 56, 2014
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2PQ2
| Structure of serine proteinase K complex with a highly flexible hydrophobic peptide at 1.8A resolution | Descriptor: | CALCIUM ION, GALAG peptide, NITRATE ION, ... | Authors: | Ethayathulla, A.S, Singh, A.K, Singh, N, Sharma, S, Sinha, M, Somvanshi, R.K, Kaur, P, Dey, S, Srinivasan, A, Singh, T.P. | Deposit date: | 2007-05-01 | Release date: | 2007-05-29 | Last modified: | 2024-10-09 | Method: | X-RAY DIFFRACTION (1.82 Å) | Cite: | Structure of serine proteinase K complex with a highly flexible hydrophobic peptide at 1.8A resolution To be Published
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