1gmk
From Proteopedia
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GRAMICIDIN/KSCN COMPLEX
Overview
The hydrophobic channel-forming polypeptide gramicidin adopts a, left-handed antiparallel double helix conformation with 6.4 residues per, turn when in complex with monovalent cation salts in a methanol, environment. The crystal structure of the gramicidin/potassium thiocyanate, complex (a = 32.06 A, b = 51.80 A, and c = 31.04 A; space group, P2(1)2(1)2(1)) has been solved to 2.5 A with an R-factor of 0.193. In the, structure, binding sites for the cations are formed by the polypeptide, backbone carbonyl groups tilting away from the helix axis toward the ions, located in the central lumen. The polypeptide backbone conformations and, the side-chain orientations in this potassium complex are significantly, different from those in the previously solved gramicidin/caesium chloride, crystal ... [(full description)]
About this Structure
1GMK is a [Protein complex] structure of sequences from [Brevibacillus brevis] with K, SCN, FOR and MOH as [ligands]. Structure known Active Sites: K2 and K4. Full crystallographic information is available from [OCA].
Reference
Crystal structure of the gramicidin/potassium thiocyanate complex., Doyle DA, Wallace BA, J Mol Biol. 1997 Mar 14;266(5):963-77. PMID:9086274
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