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Ligands
Code Name Style Show Link
LU Lutetium (III) ion
Non-standard Residues
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Glycosylation
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Code : 1PLU   PDBj   RCSB PDB   PDBe
Header : LYASE
Title : PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI WITH 1 LU+3 ION IN THE PUTATIVE CALCIUM BINDING SITE
Release Data : 1999-07-13
Compound :
mol_id molecule chains synonym
1 PROTEIN (PECTATE LYASE C) A PELC
ec: 4.2.2.2
Source :
mol_id organism_scientific
1 Erwinia chrysanthemi  (taxid:556)
strain: EC16
cellular_location: EXTRACELLULAR
plasmid: HB101
Authors : Yoder, M.D., Jurnak, F.A.
Keywords : PECTATE CLEAVAGE, PECTINOLYTIC ACTIVITY, TRANS-ELIMINATION, PARALLEL BETA-HELIX, LYASE
Exp. method : X-RAY DIFFRACTION ( 2.2 Å )
Citation :

The Refined Three-Dimensional Structure of Pectate Lyase C from Erwinia chrysanthemi at 2.2 Angstrom Resolution (Implications for an Enzymatic Mechanism).

Yoder, M.D.,Jurnak, F.
(1995)  Plant Physiol.  107 : 349 - 364

PubMed: 12228363

Chain : A
UniProt : P11073 (PLYC_DICCH)
Reaction: EC: Evidence:
Physiological Direction:
Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends. 4.2.2.2 -
-