2PEC
THE REFINED THREE-DIMENSIONAL STRUCTURE OF PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT 2.2 ANGSTROMS RESOLUTION: IMPLICATIONS FOR AN ENZYMATIC MECHANISM
Replaces: 1PECSummary for 2PEC
Entry DOI | 10.2210/pdb2pec/pdb |
Descriptor | PECTATE LYASE C (2 entities in total) |
Functional Keywords | lyase (acting on polysaccharides) |
Biological source | Erwinia chrysanthemi |
Cellular location | Secreted: P11073 |
Total number of polymer chains | 1 |
Total formula weight | 37733.61 |
Authors | Yoder, M.D.,Jurnak, F. (deposition date: 1994-08-08, release date: 1995-02-14, Last modification date: 2017-11-29) |
Primary citation | Yoder, M.D.,Jurnak, F. Protein motifs. 3. The parallel beta helix and other coiled folds. FASEB J., 9:335-342, 1995 Cited by PubMed: 7896002PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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