2j38

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|PDB= 2j38 |SIZE=350|CAPTION= <scene name='initialview01'>2j38</scene>, resolution 2.10&Aring;
|PDB= 2j38 |SIZE=350|CAPTION= <scene name='initialview01'>2j38</scene>, resolution 2.10&Aring;
|SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+A'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=GS5:5-CHLORO-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}-1-BENZOTHIOPHENE-2-SULFONAMIDE'>GS5</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GS5:5-CHLORO-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}-1-BENZOTHIOPHENE-2-SULFONAMIDE'>GS5</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Coagulation_factor_Xa Coagulation factor Xa], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.6 3.4.21.6]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Coagulation_factor_Xa Coagulation factor Xa], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.6 3.4.21.6] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j38 OCA], [http://www.ebi.ac.uk/pdbsum/2j38 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2j38 RCSB]</span>
}}
}}
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==Overview==
==Overview==
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.
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.
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==Disease==
 
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Known disease associated with this structure: Factor X deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=227600 227600]]
 
==About this Structure==
==About this Structure==
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[[Category: Senger, S.]]
[[Category: Senger, S.]]
[[Category: Watson, N S.]]
[[Category: Watson, N S.]]
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[[Category: CA]]
 
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[[Category: GS5]]
 
[[Category: blood coagulation]]
[[Category: blood coagulation]]
[[Category: calcium]]
[[Category: calcium]]
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[[Category: zymogen]]
[[Category: zymogen]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:36:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:52:18 2008''

Revision as of 00:52, 31 March 2008

Image:2j38.jpg


PDB ID 2j38

Drag the structure with the mouse to rotate
, resolution 2.10Å
Sites:
Ligands: ,
Activity: Coagulation factor Xa, with EC number 3.4.21.6
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF A HUMAN FACTOR XA INHIBITOR COMPLEX


Overview

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.

About this Structure

2J38 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Arylsulfonamides: a study of the relationship between activity and conformational preferences for a series of factor Xa inhibitors., Senger S, Convery MA, Chan C, Watson NS, Bioorg Med Chem Lett. 2006 Nov 15;16(22):5731-5. Epub 2006 Sep 18. PMID:16982192

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