2THF

STRUCTURE OF HUMAN ALPHA-THROMBIN Y225F MUTANT BOUND TO D-PHE-PRO-ARG-CHLOROMETHYLKETONE

Summary for 2THF
Related PRD IDPRD_000020
DescriptorTHROMBIN LIGHT CHAIN, THROMBIN HEAVY CHAIN, D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexan-3-yl]-L-prolinamide, ... (5 entities in total)
Functional Keywordsserine protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceHomo sapiens (human)
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Cellular locationSecreted, extracellular space: P00734 P00734
Total number of polymer chains2
Total formula weight34337.73
Authors
Caccia, S.,Futterer, K.,Di Cera, E.,Waksman, G. (deposition date: 1999-01-26, release date: 1999-03-07, Last modification date: 2013-02-27)
Primary citationCaccia, S.,Di Cera, E.,Futterer, K.,Guinto, E.R.,Rose, T.,Waksman, G.
Unexpected crucial role of residue 225 in serine proteases.
Proc.Natl.Acad.Sci.USA, 96:1852-1857, 1999
PubMed: 10051558
DOI: 110.1073/pnas.96.5.1852
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation
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PDB entries from 2021-06-16