1ai8
From Proteopedia
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HUMAN ALPHA-THROMBIN TERNARY COMPLEX WITH THE EXOSITE INHIBITOR HIRUGEN AND ACTIVE SITE INHIBITOR PHCH2OCO-D-DPA-PRO-BOROMPG
Overview
Thrombin is a multifunctional serine proteinase that plays a key role in, coagulation while exhibiting several other key cellular bioregulatory, functions. The X-ray crystal structure of human alpha-thrombin was, determined in its complex with the specific thrombin inhibitor, D-Phe-Pro-Arg chloromethylketone (PPACK) using Patterson search methods, and a search model derived from trypsinlike proteinases of known spatial, structure (Bode, W., Mayr, I., Baumann, U., Huber, R., Stone, S.R., &, Hofsteenge, J., 1989, EMBO J. 8, 3467-3475). The crystallographic, refinement of the PPACK-thrombin model has now been completed at an R, value of 0.156 (8 to 1.92 A); in particular, the amino- and the, carboxy-termini of the thrombin A-chain are now defined and all side-chain, atoms localized; only ... [(full description)]
About this Structure
1AI8 is a [Protein complex] structure of sequences from [Hirudo medicinalis] and [Homo sapiens] with T42 as [ligand]. Active as [Thrombin], with EC number [3.4.21.5]. Structure known Active Site: S1. Full crystallographic information is available from [OCA].
Reference
The refined 1.9-A X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships., Bode W, Turk D, Karshikov A, Protein Sci. 1992 Apr;1(4):426-71. PMID:1304349
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