1ytt
From Proteopedia
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|PDB= 1ytt |SIZE=350|CAPTION= <scene name='initialview01'>1ytt</scene>, resolution 1.8Å | |PDB= 1ytt |SIZE=350|CAPTION= <scene name='initialview01'>1ytt</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=YB:YTTERBIUM (III) ION'>YB</scene> | + | |LIGAND= <scene name='pdbligand=YB:YTTERBIUM+(III)+ION'>YB</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ytt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ytt OCA], [http://www.ebi.ac.uk/pdbsum/1ytt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ytt RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Flaherty, K M.]] | [[Category: Flaherty, K M.]] | ||
[[Category: Weis, W I.]] | [[Category: Weis, W I.]] | ||
| - | [[Category: YB]] | ||
[[Category: calcium dependent]] | [[Category: calcium dependent]] | ||
[[Category: carbohydrate]] | [[Category: carbohydrate]] | ||
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[[Category: recognition domain]] | [[Category: recognition domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:22:25 2008'' |
Revision as of 22:22, 30 March 2008
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| , resolution 1.8Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
YB SUBSTITUTED SUBTILISIN FRAGMENT OF MANNOSE BINDING PROTEIN-A (SUB-MBP-A), MAD STRUCTURE AT 110K
Overview
A complete and accurate set of experimental crystallographic phases to a resolution of 1.8 angstroms was obtained for a 230-residue dimeric fragment of rat mannose-binding protein A with the use of multiwavelength anomalous dispersion (MAD) phasing. An accurate image of the crystal structure could thus be obtained without resort to phases calculated from a model. Partially reduced disulfide bonds, local disorder, and differences in the mobility of chemically equivalent molecules are apparent in the experimental electron density map. A solvation layer is visible that includes well-ordered sites of hydration around polar and charged protein atoms, as well as diffuse, partially disordered solvent shells around exposed hydrophobic groups. Because the experimental phases and the resulting electron density map are free from the influence of a model, they provide a stringent test of theoretical models of macromolecular solvation, motion, and conformational heterogeneity.
About this Structure
1YTT is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Direct observation of protein solvation and discrete disorder with experimental crystallographic phases., Burling FT, Weis WI, Flaherty KM, Brunger AT, Science. 1996 Jan 5;271(5245):72-7. PMID:8539602
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