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3LIW

Factor XA in complex with (R)-2-(1-ADAMANTYLCARBAMOYLAMINO)-3-(3-CARBAMIDOYL-PHENYL)-N-PHENETHYL-PROPIONIC ACID AMIDE

Replaces:  1KYE
Summary for 3LIW
Entry DOI10.2210/pdb3liw/pdb
DescriptorActivated factor Xa heavy chain, Factor X light chain, CALCIUM ION, ... (5 entities in total)
Functional Keywordscoagulation factor inhibitor, factor xa, hydrolase, blood coagulation, calcium, cleavage on pair of basic residues, disulfide bond, egf-like domain, gamma-carboxyglutamic acid, glycoprotein, hydroxylation, polymorphism, protease, secreted, serine protease, zymogen
Biological sourceHomo sapiens (human)
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Cellular locationSecreted: P00742 P00742
Total number of polymer chains2
Total formula weight32474.95
Authors
Mueller, M.M.,Sperl, S.,Sturzebecher, J.,Bode, W.,Moroder, L. (deposition date: 2010-01-25, release date: 2010-04-07, Last modification date: 2023-09-06)
Primary citationMueller, M.M.,Sperl, S.,Sturzebecher, J.,Bode, W.,Moroder, L.
(R)-3-Amidinophenylalanine-Derived Inhibitors of Factor Xa with a Novel Active-Site Binding Mode
Biol.Chem., 383:1185-, 2003
Cited by
PubMed Abstract: A putative non-substrate like binding mode of (R)-3-amidinophenylalanine derivatives to factor Xa, as derived from modeling experiments based on X-ray analysis of their complexes with trypsin, was used to design a new generation of inhibitors. However, the resulting inhibitory potencies were not at all consistent with the working assumption, although with an adamantyl-ureido derivative of (R)-3-amidinophenylalanine phenetyl amide a highly selective nanomolar inhibition of factor Xa was achieved. The X-ray analysis of the complex of this ligand with factor Xa revealed an unexpected new binding mode, of which the most important feature is the interaction of the C-terminal aryl moiety with a hydrophobic subregion of the S1 subsite, while the adamantyl group occupies the hydrophobic S3/S4 subsites of the enzyme.
PubMed: 12437104
DOI: 10.1515/BC.2002.130
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.22 Å)
Structure validation

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