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MineSummary [1qf0]

Summary Structural Experimental Function Sequence Neighbor Download Link

<Asymmetric unit>
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PDB ID1qf0  sequence information (FASTA format)   
DescriptorTHERMOLYSIN (E.C.3.4.24.27)
TitleTHERMOLYSIN (E.C.3.4.24.27) COMPLEXED WITH (2-SULPHANYL-3-PHENYLPROPANOYL)-PHE-TYR. PARAMETERS FOR ZN-BIDENTATION OF MERCAPTOACYLDIPEPTIDES IN METALLOENDOPEPTIDASE
Functional KeywordsNEUTRAL ENDOPEPTIDASE, ZN METALLOPEPTIDASE, HYDROLASE
Biological sourceBacillus thermoproteolyticus
Cellular location [UNP - P00800] Secreted
Total number of polymer chains1
Total molecular weight35237.2 (the details in Structural Details Page)
AuthorsGaucher, J.-F. , Selkti, M. , Tiraboschi, G. , Prange, T. , Roques, B.P. , Tomas, A. , Fournie-Zaluski, M.C. (deposition date : 1999-04-06, release date : 1999-12-29)
Primary citationGaucher, J.F. , Selkti, M. , Tiraboschi, G. , Prange, T. , Roques, B.P. , Tomas, A. , Fournie-Zaluski, M.C.
Crystal structures of alpha-mercaptoacyldipeptides in the thermolysin active site: structural parameters for a Zn monodentation or bidentation in metalloendopeptidases.
Biochemistry, 38:12569 - 12576, 1999.(PubMed : 10504225)  (DOI: 10.1021/bi991043z)
Experimental methodX-RAY DIFFRACTION ( 2.20[Å] )
Other Database Information
Yorodumi , CATH , CE , FSSP , SCOP , VAST , UniProt ( P00800 ) , eF-site , KEGG ( EC 3.4.24.27 ) , PISA