Editing Factor X (section)

== Structure ==
{{See also|Factor IX#Domain architecture}}
The first crystal structure of human factor Xa was deposited in May 1993. To date, 191 crystal structures of factor Xa with various inhibitors have been deposited in the protein data bank. The active site of factor Xa is divided into four subpockets as S1, S2, S3 and S4. The S1 subpocket determines the major component of selectivity and binding. The S2 sub-pocket is small, shallow and not well defined. It merges with the S4 subpocket. The S3 sub-pocket is located on the rim of the S1 pocket and is quite exposed to solvent. The S4 sub-pocket has three ligand binding domains: the "hydrophobic box", the "cationic hole" and the water site. Factor Xa inhibitors generally bind in an L-shaped conformation, where one group of the ligand occupies the anionic S1 pocket lined by residues [[Aspartic acid|Asp]]189, [[Serine|Ser]]195, and [[Tyrosine|Tyr]]228, and another group of the ligand occupies the aromatic S4 pocket lined by residues Tyr99, [[Phenylalanine|Phe]]174, and Trp215. Typically, a fairly rigid linker group bridges these two interaction sites.<ref>{{Cite web |url=http://pharmaxchange.info/presentations/Direct%20FXa%20Inhibitors.html |title=Presentation on Direct Factor Xa Inhibitors |access-date=2010-04-08 |archive-url=https://web.archive.org/web/20160303184211/http://pharmaxchange.info/presentations/Direct%20FXa%20Inhibitors.html |archive-date=2016-03-03 |url-status=dead }}</ref>