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[8tln] replaced from '3tln'

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<Asymmetric unit>
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PDB ID8tln  sequence information (FASTA format)   
DescriptorTHERMOLYSIN (E.C.3.4.24.27) COMPLEXED WITH VAL-LYS DIPEPTIDE
TitleSTRUCTURAL COMPARISON SUGGESTS THAT THERMOLYSIN AND RELATED NEUTRAL PROTEASES UNDERGO HINGE-BENDING MOTION DURING CATALYSIS
Functional KeywordsHYDROLASE(METALLOPROTEINASE)
Biological sourceBacillus thermoproteolyticus
Cellular location [UNP - P00800] Secreted
Total number of polymer chains1
Total molecular weight34930.8 (the details in Structural Details Page)
AuthorsTronrud, D. , Matthews, B.W. (deposition date : 1993-09-01, release date : 1994-04-30)
Primary citationHolland, D.R. , Tronrud, D.E. , Pley, H.W. , Flaherty, K.M. , Stark, W. , Jansonius, J.N. , McKay, D.B. , Matthews, B.W.
Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis.
Biochemistry, 31:11310 - 11316, 1992.(PubMed : 1445869)  (DOI: 10.1021/bi00161a008)
Experimental methodX-RAY DIFFRACTION ( 1.6[Å] )
Other Database Information
Yorodumi , CATH , CE , FSSP , SCOP , VAST , UniProt ( P00800 ) , eF-site , KEGG ( EC 3.4.24.27 ) , PISA