1PCL
UNUSUAL STRUCTURAL FEATURES IN THE PARALLEL BETA-HELIX IN PECTATE LYASES
Summary for 1PCL
Entry DOI | 10.2210/pdb1pcl/pdb |
Descriptor | PECTATE LYASE E (1 entity in total) |
Functional Keywords | lyase (acting on polysaccharides) |
Biological source | Erwinia chrysanthemi |
Cellular location | Secreted: P04960 |
Total number of polymer chains | 1 |
Total formula weight | 38216.22 |
Authors | Lietzke, S.E.,Keen, N.T.,Jurnak, F. (deposition date: 1993-11-05, release date: 1995-02-14, Last modification date: 2024-02-14) |
Primary citation | Yoder, M.D.,Lietzke, S.E.,Jurnak, F. Unusual structural features in the parallel beta-helix in pectate lyases. Structure, 1:241-251, 1993 Cited by PubMed Abstract: A new type of domain structure, an all parallel beta class, has recently been observed in two pectate lyases, PelC and PelE. The atomic models have been analyzed to determine whether the new tertiary fold exhibits unusual structural features. PubMed: 8081738DOI: 10.1016/0969-2126(93)90013-7 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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