1C4D
GRAMICIDIN CSCL COMPLEX
Summary for 1C4D
Entry DOI | 10.2210/pdb1c4d/pdb |
Related | 1AL4 1ALX 1ALZ 1AV2 1BDW 1GMK 1GRM 1JNO 1JO3 1JO4 1KQE 1MAG 1MIC 1NG8 1NRM 1NRU 1NT5 1NT6 1TK2 1TKQ 1W5U 2IZQ 2XDC 3L8L |
Related PRD ID | PRD_000150 |
Descriptor | GRAMICIDIN A, CESIUM ION, CHLORIDE ION, ... (5 entities in total) |
Functional Keywords | antibiotic, gramicidin, antifungal, antibacterial, double helix, membrane ion channel, linear gramicidin |
Biological source | BREVIBACILLUS BREVIS |
Total number of polymer chains | 4 |
Total formula weight | 9221.68 |
Authors | Wallace, B.A. (deposition date: 1999-06-04, release date: 2000-01-03, Last modification date: 2024-10-16) |
Primary citation | Wallace, B.A.,Ravikumar, K. The Gramicidin Pore: Crystal Structure of a Cesium Complex. Science, 241:182-, 1988 Cited by PubMed Abstract: Gramicidin, a linear polypeptide composed of hydrophobic amino acids with alternating L- and D- configurations, forms transmembrane ion channels. The crystal structure of a gramicidin-cesium complex has been determined at 2.0 angstrom resolution. In this structure, gramicidin forms a 26 angstrom long tube comprised of two polypeptide chains arranged as antiparallel beta strands that are wrapped into a left-handed helical coil with 6.4 residues per turn. The polypeptide backbone forms the interior of the hydrophilic, solvent-filled pore and the side chains form a hydrophobic and relatively regular surface on the outside of the pore. This example of a crystal structure of a solvent-filled ion pore provides a basis for understanding the physical nature of ion translocation. PubMed: 2455344DOI: 10.1126/SCIENCE.2455344 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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