2J38

CRYSTAL STRUCTURE OF A HUMAN FACTOR XA INHIBITOR COMPLEX

Summary for 2J38

• Entry DOI: 10.2210/pdb2j38/pdb
• Related: 1C5M 1EZQ 1F0R 1F0S 1FAX 1FJS 1FXY 1G2L 1G2M 1HCG 1IOE 1IQE 1IQF 1IQG 1IQH 1IQI 1IQJ 1IQK 1IQL 1IQM 1IQN 1KSN 1KYE 1LPG 1LPK 1LPZ 1LQD 1MQ5 1MQ6 1MSX 1NFU 1NFW 1NFX 1NFY 1NL8 1P0S 1V3X 1WU1 1XKA 1XKB 1Z6E 2BMG 2BOH 2BOK 2BQ6 2BQ7 2BQW 2CJI 2FZZ 2GD4 2J2U 2J34
• Descriptor: ACTIVATED FACTOR XA HEAVY CHAIN, FACTOR X LIGHT CHAIN, 5-CHLORO-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}-1-BENZOTHIOPHENE-2-SULFONAMIDE, ... (5 entities in total)
• Functional Keywords: gamma- carboxyglutamic acid, serine protease, egf-like domain, blood coagulation, polymorphism, glycoprotein, hydroxylation, gamma-carboxyglutamic acid, calcium, zymogen, complex, protease, hydrolase
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Secreted: P00742 P00742
• Total number of polymer chains: 2
• Total formula weight: 44273.45

Authors

Senger, S.,Convery, M.A.,Chan, C.,Watson, N.S. (deposition date: 2006-08-18, release date: 2006-09-27, Last modification date: 2023-12-13)

Primary citation

Senger, S.,Convery, M.A.,Chan, C.,Watson, N.S.
Arylsulfonamides: A Study of the Relationship between Activity and Conformational Preferences for a Series of Factor Xa Inhibitors.
Bioorg.Med.Chem.Lett., 16:5731-, 2006

PubMed Abstract: Torsional scans of sulfonamide S-C bonds in small model systems of a series of arylsulfonamide factor Xa inhibitors were performed in order to investigate if conformational effects can help to rationalise the observed SAR. Computational results were in good agreement with the experimental data indicating that the sulfonamide conformation plays an important role in determining the activity in this particular series of factor Xa inhibitors.

PubMed: 16982192
DOI: 10.1016/J.BMCL.2006.08.092

Experimental method

X-RAY DIFFRACTION (2.1 Å)