1ncx
From Proteopedia
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|PDB= 1ncx |SIZE=350|CAPTION= <scene name='initialview01'>1ncx</scene>, resolution 1.8Å | |PDB= 1ncx |SIZE=350|CAPTION= <scene name='initialview01'>1ncx</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> | + | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ncx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ncx OCA], [http://www.ebi.ac.uk/pdbsum/1ncx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ncx RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Rao, S T.]] | [[Category: Rao, S T.]] | ||
[[Category: Sundaralingam, M.]] | [[Category: Sundaralingam, M.]] | ||
| - | [[Category: CD]] | ||
| - | [[Category: SO4]] | ||
[[Category: calcium-binding protein]] | [[Category: calcium-binding protein]] | ||
[[Category: duplication]] | [[Category: duplication]] | ||
[[Category: muscle protein]] | [[Category: muscle protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:28:36 2008'' |
Revision as of 19:28, 30 March 2008
| |||||||
| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
TROPONIN C
Overview
The crystal structures of three metal complexes of troponin C (TnC) have been determined and refined where the two occupied structural Ca(2+) sites in the C domain have been substituted by Mn(2+), Cd(2+) and Tb(3+). The X-ray intensity data were collected to 2.1, 1.8 and 1.8 A resolution, respectively, on the three metal complexes, which are isomorphous with Ca-TnC. The three complexes have r.m.s. deviations of 0.27, 0.25 and 0.35 A, respectively, for all protein atoms, from Ca-TnC. Irrespective of the charge on the metal (+2 or +3), the occupied sites 3 and 4 exhibit a distorted pentagonal bipyramidal coordination, like Ca-TnC, with seven ligands, six from the 12-residue binding loop and the seventh from a water molecule. Mn(2+) at site 4 seems to display a longer distance to one of the carboxyl bidentate ligands representing an intermediate coordination simulating the six-coordinate Mg(2+). The carboxyl O atoms of the bidentate Glu12 are displaced on the side of the equatorial plane passing through the remaining three ligands with one O atom closer to the plane (Delta of 0.11 to 0.76 A) than the other (Delta of 0.93 to 1.38 A). The two axial ligands are an aspartic carboxyl O atom and a water molecule. The metal is displaced (0.18 to 0.56 A) towards the water facing the water channel.
About this Structure
1NCX is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
X-ray structures of Mn, Cd and Tb metal complexes of troponin C., Rao ST, Satyshur KA, Greaser ML, Sundaralingam M, Acta Crystallogr D Biol Crystallogr. 1996 Sep 1;52(Pt 5):916-22. PMID:15299599
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