SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborDownloads

2JET

CRYSTAL STRUCTURE OF A TRYPSIN-LIKE MUTANT (S189D, A226G) CHYMOTRYPSIN.

Summary for 2JET

Related1KDQ 
DescriptorCHYMOTRYPSINOGEN B CHAIN A (E.C.3.4.21.1), CHYMOTRYPSINOGEN B CHAIN B (E.C.3.4.21.1), CHYMOTRYPSINOGEN B CHAIN C (E.C.3.4.21.1)
Functional KeywordsSUBSTRATE SPECIFICITY, ZYMOGEN, PROTEASE, HYDROLASE, DIGESTION, SERINE PROTEASE, PROTEIN ENGINEERING,HYDROLASE
Biological sourceRATTUS NORVEGICUS (RAT)
Cellular locationSecreted, extracellular space 
Total number of polymer chains3
Total molecular weight25679.25
Authors
Jelinek, B.,Katona, G.,Fodor, K.,Venekei, I.,Graf, L. (deposition date: 2007-01-22, release date: 2007-09-18, modification date: 2011-07-13)
Primary citation
Jelinek, B.,Katona, G.,Fodor, K.,Venekei, I.,Graf, L.
The Crystal Structure of a Trypsin-Like Mutant Chymotrypsin: The Role of Position 226 in the Activity and Specificity of S189D Chymotrypsin.
Protein J., 27:79-, 2008
PubMed: 17805946
DOI: 10.1007/S10930-007-9110-3
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.2 Å)

More Asymmetric unit images

no rotation
rotated about x axis by 90°
rotated about y axis by 90°
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entries available on 2014-09-17
00:00 UTC / 09:00 JST