This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1whe
From Proteopedia
(Difference between revisions)
m (Protected "1whe" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
[[Image:1whe.png|left|200px]] | [[Image:1whe.png|left|200px]] | ||
| - | <!-- | ||
| - | The line below this paragraph, containing "STRUCTURE_1whe", creates the "Structure Box" on the page. | ||
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet) | ||
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | ||
| - | or leave the SCENE parameter empty for the default display. | ||
| - | --> | ||
{{STRUCTURE_1whe| PDB=1whe | SCENE= }} | {{STRUCTURE_1whe| PDB=1whe | SCENE= }} | ||
===COAGULATION FACTOR, NMR, 20 STRUCTURES=== | ===COAGULATION FACTOR, NMR, 20 STRUCTURES=== | ||
| - | |||
| - | <!-- | ||
| - | The line below this paragraph, {{ABSTRACT_PUBMED_8794734}}, adds the Publication Abstract to the page | ||
| - | (as it appears on PubMed at http://www.pubmed.gov), where 8794734 is the PubMed ID number. | ||
| - | --> | ||
{{ABSTRACT_PUBMED_8794734}} | {{ABSTRACT_PUBMED_8794734}} | ||
Revision as of 08:02, 20 June 2012
Contents |
COAGULATION FACTOR, NMR, 20 STRUCTURES
Template:ABSTRACT PUBMED 8794734
About this Structure
1whe is a 1 chain structure of Factor Xa with sequence from Bos taurus. Full experimental information is available from OCA.
See Also
Reference
- Sunnerhagen M, Olah GA, Stenflo J, Forsen S, Drakenberg T, Trewhella J. The relative orientation of Gla and EGF domains in coagulation factor X is altered by Ca2+ binding to the first EGF domain. A combined NMR-small angle X-ray scattering study. Biochemistry. 1996 Sep 10;35(36):11547-59. PMID:8794734 doi:10.1021/bi960633j
