1EVR
The structure of the resorcinol/insulin R6 hexamer
Summary for 1EVR
| Entry DOI | 10.2210/pdb1evr/pdb |
| Related | 1EV3 1EV6 |
| Descriptor | INSULIN, RESORCINOL, ZINC ION, ... (7 entities in total) |
| Functional Keywords | r6 insulin hexamer, hormone-growth factor complex, hormone/growth factor |
| Cellular location | Secreted: P01308 P01308 |
| Total number of polymer chains | 12 |
| Total formula weight | 36011.51 |
| Authors | Smith, G.D.,Ciszak, E.,Magrum, L.A.,Pangborn, W.A.,Blessing, R.H. (deposition date: 2000-04-20, release date: 2000-12-04, Last modification date: 2024-10-30) |
| Primary citation | Smith, G.D.,Ciszak, E.,Magrum, L.A.,Pangborn, W.A.,Blessing, R.H. R6 hexameric insulin complexed with m-cresol or resorcinol. Acta Crystallogr.,Sect.D, 56:1541-1548, 2000 Cited by PubMed Abstract: The structures of three R(6) human insulin hexamers have been determined. Crystals of monoclinic m-cresol-insulin, monoclinic resorcinol-insulin and rhombohedral m-cresol-insulin diffracted to 1. 9, 1.9 and 1.78 A, respectively, and have been refined to residuals of 0.195, 0.179 and 0.200, respectively. In all three structures, a phenolic derivative is found to occupy the phenolic binding site, where it forms hydrogen bonds to the carbonyl O atom of CysA6 and the N atom of CysA11. Two additional phenolic derivative binding sites were identified within or between hexamers. The structures of all three hexamers are nearly identical, although a large displacement of the N-terminus of one B chain in both monoclinic structures results from coordination to a sodium ion which is located between symmetry-related hexamers. Other minor differences in structure arise from differences in packing in the monoclinic cell compared with the rhombohedral cell. Based upon the differences in conformation of the GluB13 side chains in T(6), T(3)R(f)(3) and R(6) hexamers, the deprotonation of these side chains appears to be associated with the T-->R conformational transition. PubMed: 11092919DOI: 10.1107/S0907444900012749 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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