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MineSummary [1gec]

Summary Structural Experimental Function Sequence Neighbor Download Link

<Asymmetric unit>
= <Biological unit>
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PDB ID1gec  sequence information (FASTA format)   
RELATED PRD_IDPRD_000337
DescriptorGLYCYL ENDOPEPTIDASE, BENZYLOXYCARBONYL-LEUCINE-VALINE-GLYCINE-METHYLENE
TitleGLYCYL ENDOPEPTIDASE-COMPLEX WITH BENZYLOXYCARBONYL-LEUCINE-VALINE-GLYCINE-METHYLENE COVALENTLY BOUND TO CYSTEINE 25
Functional KeywordsPROTEINASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
HYDROLASE/HYDROLASE INHIBITOR
Biological sourceCarica papaya (papaya)
Organ source [UNP - P05994] Leaf
Total number of polymer chains2
Total molecular weight23808.3 (the details in Structural Details Page)
AuthorsOhara, B.P. , Hemmings, A.M. , Buttle, D.J. , Pearl, L.H. (deposition date : 1995-05-25, release date : 1995-12-07, last modified : 2011-07-13)
Primary citationO'Hara, B.P. , Hemmings, A.M. , Buttle, D.J. , Pearl, L.H.
Crystal structure of glycyl endopeptidase from Carica papaya: a cysteine endopeptidase of unusual substrate specificity.
Biochemistry, 34:13190 - 13195, 1995.(PubMed : 7548082)  (DOI: 10.1021/bi00040a034)
Experimental methodX-RAY DIFFRACTION ( 2.1[Å] )
Other Database Information
Yorodumi , CATH , FSSP , SCOP , VAST , UniProt ( P05994 ) , eF-site , KEGG (EC 3.4.22.25 ) , PISA , wwPDB/RDF


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