1QBO
BOVINE TRYPSIN 7-[[6-[[1-(1-IMINOETHYL)PIPERIDIN-4-YL]OXY]-2-METHYL-BENZIMIDAZOL-1-YL]METHYL]NAPHTHALENE-2-CARBOXIMIDAMID ZK-806711 INHIBITOR COMPLEX
Summary for 1QBO
| Entry DOI | 10.2210/pdb1qbo/pdb |
| Descriptor | PROTEIN (TRYPSIN), CALCIUM ION, 7-[[6-[[1-(1-IMINOETHYL)PIPERIDIN-4-YL]OXY]-2-METHYL-BENZIMIDAZOL-1-YL]METHYL]NAPHTHALENE-2-CARBOXIMIDAMID, ... (4 entities in total) |
| Functional Keywords | factor xa, inhibitor complex, hydrolase, serine proteinase |
| Biological source | Bos taurus (cattle) |
| Cellular location | Secreted, extracellular space: P00760 |
| Total number of polymer chains | 1 |
| Total formula weight | 23860.02 |
| Authors | Whitlow, M. (deposition date: 1999-04-26, release date: 2000-05-03, Last modification date: 2024-10-16) |
| Primary citation | Whitlow, M.,Arnaiz, D.O.,Buckman, B.O.,Davey, D.D.,Griedel, B.,Guilford, W.J.,Koovakkat, S.K.,Liang, A.,Mohan, R.,Phillips, G.B.,Seto, M.,Shaw, K.J.,Xu, W.,Zhao, Z.,Light, D.R.,Morrissey, M.M. Crystallographic analysis of potent and selective factor Xa inhibitors complexed to bovine trypsin. Acta Crystallogr.,Sect.D, 55:1395-1404, 1999 Cited by PubMed Abstract: Factor Xa is a serine protease which activates thrombin (factor IIa) and plays a key regulatory role in the blood-coagulation cascade. Factor Xa is, therefore, an important target for the design of anti-thrombotics. Both factor Xa and thrombin share sequence and structural homology with trypsin. As part of a factor Xa inhibitor-design program, a number of factor Xa inhibitors were crystallographically studied complexed to bovine trypsin. The structures of one diaryl benzimidazole, one diaryl carbazole and three diaryloxypyridines are described. All five compounds bind to trypsin in an extended conformation, with an amidinoaryl group in the S1 pocket and a second basic/hydrophobic moiety bound in the S4 pocket. These binding modes all bear a resemblance to the reported binding mode of DX-9065a in bovine trypsin and human factor Xa. PubMed: 10417407DOI: 10.1107/S0907444999007350 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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