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From Proteopedia
Serine Protease - Thrombin
Thrombin is a "trypsin-like" serine protease. The Active site of thrombin is made up of a catalytic triad of Ser195, His57 and Asp102. At the activation site, the sidechain of Asp194 makes a salt link with the N-terminus at residue 16. Thrombin is proteolytically cleaved to form thrombin in the first step of the coagulation cascade which ultimately results in the stemming of blood loss. It also converts soluble fibrinogen into insoluble strands of fibrin. It also catalyzes many other reactions.
The B chain consists of two domains. As is true for all of the "trypsin-like" serine proteases, each of the two thrombin domains consists mainly of a 6-stranded, antiparallel beta barrel.
Jordan Ferguson and Shane Evans
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| 2age, resolution 1.15Å () | |||||||||
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| Non-Standard Residues: | |||||||||
| Activity: | Trypsin, with EC number 3.4.21.4 | ||||||||
| Related: | 2agg, 2agi, 2ah4
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
