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UNUSUAL STRUCTURAL FEATURES IN THE PARALLEL BETA-HELIX IN PECTATE LYASES[LYASE (ACTING ON POLYSACCHARIDES)]
View in iCn3D Similar StructuresPubMedProteinsConserved Domains
MUTATIONS IN THE T1.5 LOOP OF PECTATE LYASE A[LYASE]
Mutations in the T1.5 loop of pectate lyase A[LYASE]
Crystal Structure of Pectate Lyase A (C2 form)[LYASE]
View in iCn3D Similar StructuresPubMedProteinsConserved DomainsPubChem Compound
Crystal Structure of the R3 form of Pectate Lyase A, Erwinia chrysanthemi[LYASE]
BACILLUS SUBTILIS PECTATE LYASE[LYASE]
BACILLUS SUBTILIS PECTATE LYASE R279K MUTANT[LYASE]
View in iCn3D Similar StructuresProteinsConserved DomainsPubChem Compound
Structure of the thermostable pectate lyase PL 47[LYASE]
Pectate lyase bound to trisaccharide[LYASE]
Pectate lyase bound to hexasaccharide[LYASE]
Pectate lyase bound to hexasaccharide compound IV[LYASE]
Pectate lyase bound to hexasaccharide compound III[LYASE]
Pectate lyase bound to hexasaccharide compound II[LYASE]
Hexasaccharide I bound to Bacillus subtilis pectate lyase[LYASE]
Structural insights into substrate specificity and the anti beta-elimination mechanism of pectate lyase[LYASE]
1.7 Angstrom Crystal Structure of jun a 1, the major allergen from cedar pollen[ALLERGEN]
THE REFINED THREE-DIMENSIONAL STRUCTURE OF PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT 2.2 ANGSTROMS RESOLUTION: IMPLICATIONS FOR AN ENZYMATIC MECHANISM[LYASE (ACTING ON POLYSACCHARIDES)]
PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI (EC16) TO A RESOLUTION OF 2.2 ANGSTROMS WITH 128 WATERS[PECTATE CLEAVAGE]
Pectate Lyase C from Erwinia Chrysanthemi at pH 4.5 with no Ca2+ Added[HYDROLASE]
Pectate Lyase C from Erwinia Chrysanthemi at pH 4.5 with 5mM CA2+[HYDROLASE]
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