9B1U
| Crystal structure of PqqT with PQQ bound | Descriptor: | PYRROLOQUINOLINE QUINONE, Putative ABC transporter periplasmic solute-binding protein, SODIUM ION | Authors: | Boggs, D, Bruchs, A, Thompson, P, Olshansky, L, Bridwell-Rabb, J. | Deposit date: | 2024-03-13 | Release date: | 2024-08-21 | Method: | X-RAY DIFFRACTION (1.46 Å) | Cite: | Structure-driven development of a biomimetic rare earth artificial metalloprotein. Proc.Natl.Acad.Sci.USA, 121, 2024
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9B1V
| Crystal structure of PqqT with PQQ and Gd3+ bound | Descriptor: | 1,2-ETHANEDIOL, GADOLINIUM ION, PYRROLOQUINOLINE QUINONE, ... | Authors: | Boggs, G.D, Bruchs, A.T, Thompson, P.J, Olshansky, L, Bridwell-Rabb, J. | Deposit date: | 2024-03-13 | Release date: | 2024-08-21 | Method: | X-RAY DIFFRACTION (1.55 Å) | Cite: | Structure-driven development of a biomimetic rare earth artificial metalloprotein. Proc.Natl.Acad.Sci.USA, 121, 2024
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7UZO
| Parathyroid hormone 1 receptor extracellular domain complexed with a peptide ligand containing one beta-amino acid | Descriptor: | Parathyroid hormone/parathyroid hormone-related peptide receptor, Peptide from Parathyroid hormone-related protein, ZINC ION | Authors: | Yu, Z, Bruchs, A.T, Bingman, C.A, Gellman, S.H. | Deposit date: | 2022-05-09 | Release date: | 2022-10-19 | Last modified: | 2023-11-15 | Method: | X-RAY DIFFRACTION (1.3 Å) | Cite: | Altered signaling at the PTH receptor via modified agonist contacts with the extracellular domain provides a path to prolonged agonism in vivo. Proc.Natl.Acad.Sci.USA, 119, 2022
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7UZP
| parathyroid hormone 1 receptor extracellular domain complexed with a peptide ligand containing three beta-amino acids | Descriptor: | 1,2-ETHANEDIOL, PTHrP[1-36] 24,28,31 XCP, Parathyroid hormone/parathyroid hormone-related peptide receptor, ... | Authors: | Yu, Z, Bruchs, A.T, Bingman, C.A, Gellman, S.H. | Deposit date: | 2022-05-09 | Release date: | 2022-10-19 | Last modified: | 2024-02-28 | Method: | X-RAY DIFFRACTION (2.29 Å) | Cite: | Altered signaling at the PTH receptor via modified agonist contacts with the extracellular domain provides a path to prolonged agonism in vivo. Proc.Natl.Acad.Sci.USA, 119, 2022
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