3ebx

REFINEMENT AT 1.4 ANGSTROMS RESOLUTION OF A MODEL OF ERABUTOXIN B. TREATMENT OF ORDERED SOLVENT AND DISCRETE DISORDER

spinqualitylabelsall models 3ebx, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ebx is a 1 chain structure with sequence from Black-banded sea krait. This structure supersedes the now removed PDB entry 2ebx. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 Related: 5ebx Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [NXSB_PSSEM] Binds with high affinity to muscular nicotinic acetylcholine receptors (nAChRs), and with low affinity to neuronal alpha-7 nAChRs and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The latter stages in the refinement of the protein erabutoxin b are described. The crystal structure of the 62-residue protein has been refined to a conventional R factor of 0.144 by stereochemically restrained least-squares methods using diffraction data to a limit of 1.4 A spacings. Emphasis was placed on determining as accurately as possible the solvent structure and the structures of heterogeneous groups in the protein. The final model includes two conformers for each of seven side chains and for an octapeptide segment. A total of 111 sites for water molecules have been located as well as one sulfate ion with a total of 68 site occupancies. 65 of the solvent sites overlap either with protein atoms belonging to groups in two alternative conformations or with other solvent sites. Dual protein conformers and overlapping solvent sites were both included in the least-squares refinement. Individual thermal and occupancy parameters were refined for solvent molecules. An analysis of these parameters has provided useful structural information. Refinement at 1.4 A resolution of a model of erabutoxin b: treatment of ordered solvent and discrete disorder.,Smith JL, Corfield PW, Hendrickson WA, Low BW Acta Crystallogr A. 1988 May 1;44 ( Pt 3):357-68. PMID:3272151 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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