7T8T
| CryoEM structure of PLCg1 | Descriptor: | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma, CALCIUM ION | Authors: | Endo-Streeter, S, Sondek, J. | Deposit date: | 2021-12-17 | Release date: | 2022-12-21 | Last modified: | 2024-06-05 | Method: | ELECTRON MICROSCOPY (3.68 Å) | Cite: | CryoEM structure of PLCg1 To Be Published
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7SQ2
| Reprocessed and refined structure of Phospholipase C-beta and Gq signaling complex | Descriptor: | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3, ACETATE ION, CALCIUM ION, ... | Authors: | Endo-Streeter, S.T, Sondek, J, Harden, T.K. | Deposit date: | 2021-11-04 | Release date: | 2021-11-17 | Last modified: | 2023-10-18 | Method: | X-RAY DIFFRACTION (2.6 Å) | Cite: | Kinetic Scaffolding Mediated by a Phospholipase C-{beta} and Gq Signaling Complex Science, 330, 2010
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4FRF
| Structural Studies and Protein Engineering of Inositol Phosphate Multikinase | Descriptor: | Inositol polyphosphate multikinase alpha, SULFATE ION | Authors: | Endo-Streeter, S.T, Tsui, M, Odom, A.R, York, J.D. | Deposit date: | 2012-06-26 | Release date: | 2012-08-15 | Last modified: | 2024-02-28 | Method: | X-RAY DIFFRACTION (2.9 Å) | Cite: | Structural studies and protein engineering of inositol phosphate multikinase. J.Biol.Chem., 287, 2012
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6WRR
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6WRY
| CRYSTAL STRUCTURE OF INOSITOL POLYPHOSPHATE 1-PHOSPHATASE INPP1 IN COMPLEX GADOLINIUM AFTER ADDITION OF INOSITOL 1,3,4-TRISPHOSPHATE AT 2.5 ANGSTROM RESOLUTION | Descriptor: | GADOLINIUM ATOM, Inositol polyphosphate 1-phosphatase, SULFATE ION | Authors: | Dollins, D.R, Endo-Streeter, S, York, J.D. | Deposit date: | 2020-04-30 | Release date: | 2020-11-25 | Last modified: | 2023-10-18 | Method: | X-RAY DIFFRACTION (2.8 Å) | Cite: | A structural basis for lithium and substrate binding of an inositide phosphatase. J.Biol.Chem., 296, 2020
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6X25
| CRYSTAL STRUCTURE OF INOSITOL POLYPHOSPHATE 1-PHOSPHATASE INPP1 IN COMPLEX GADOLINIUM AFTER ADDITION OF INOSITOL 1,3,4-TRISPHOSPHATE AND LITHIUM AT 3.2 ANGSTROM RESOLUTION | Descriptor: | GADOLINIUM ATOM, Inositol polyphosphate 1-phosphatase, SULFATE ION | Authors: | Dollins, D.E, Endo-Streeter, S, Ren, Y, York, J.D. | Deposit date: | 2020-05-20 | Release date: | 2020-11-25 | Last modified: | 2023-10-18 | Method: | X-RAY DIFFRACTION (3.2 Å) | Cite: | A structural basis for lithium and substrate binding of an inositide phosphatase. J.Biol.Chem., 296, 2020
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6WRO
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4HNW
| The NatA Acetyltransferase Complex Bound To Inositol Hexakisphosphate | Descriptor: | INOSITOL HEXAKISPHOSPHATE, N-terminal acetyltransferase A complex catalytic subunit ARD1, N-terminal acetyltransferase A complex subunit NAT1, ... | Authors: | Neubauer, J.L, Immormino, R.M, Dollins, D.E, Endo-Streeter, S.T, Pemble IV, C.W, York, J.D. | Deposit date: | 2012-10-21 | Release date: | 2014-03-26 | Last modified: | 2024-02-28 | Method: | X-RAY DIFFRACTION (2.801 Å) | Cite: | The Protein Complex NatA Binds Inositol Hexakisphosphate and Exhibits Conformational Flexibility To be Published
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4HNY
| Apo N-terminal acetyltransferase complex A | Descriptor: | GLYCEROL, N-terminal acetyltransferase A complex catalytic subunit ARD1, N-terminal acetyltransferase A complex subunit NAT1, ... | Authors: | Neubauer, J.L, Immormino, R.M, Dollins, D.E, Endo-Streeter, S.T, Pemble IV, C.W, York, J.D. | Deposit date: | 2012-10-21 | Release date: | 2014-03-26 | Method: | X-RAY DIFFRACTION (2.249 Å) | Cite: | The Protein Complex NatA Binds Inositol Hexakisphosphate and Exhibits Conformational Flexibility To be Published
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4HNX
| The NatA Acetyltransferase Complex Bound To ppGpp | Descriptor: | GUANOSINE-5',3'-TETRAPHOSPHATE, N-terminal acetyltransferase A complex catalytic subunit ARD1, N-terminal acetyltransferase A complex subunit NAT1 | Authors: | Neubauer, J.L, Immormino, R.M, Dollins, D.E, Endo-Streeter, S.T, Pemble IV, C.W, York, J.D. | Deposit date: | 2012-10-21 | Release date: | 2014-03-26 | Last modified: | 2024-02-28 | Method: | X-RAY DIFFRACTION (2.339 Å) | Cite: | The Protein Complex NatA Binds Inositol Hexakisphosphate and Exhibits Conformational Flexibility To be Published
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