2pec Summary

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PDB entry 2pec (supersedes 1pec)

THE REFINED THREE-DIMENSIONAL STRUCTURE OF PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT 2.2 ANGSTROMS RESOLUTION: IMPLICATIONS FOR AN ENZYMATIC MECHANISM

The structure was published by Yoder, M.D. and Jurnak, F., in 1995 in a paper entitled "Protein motifs. 3. The parallel beta helix and other coiled folds." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 1994.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of PECTATE LYASE C. This molecule has the UniProt identifier P11073 (PLYC_ERWCH)search. The sample contained 353 residues which is 100% of the natural sequence. Out of 353 residues 352 were observed and are deposited in the PDB.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A PECTATE LYASE C P11073 (23-375) (PLYC_ERWCH)search Erwinia chrysanthemisearch 100% 353 99%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P11073 (23 - 375) PECTATE LYASE C Erwinia chrysanthemi

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P11073) Pectate lyase-likesearch Single-stranded right-handed beta-helix, Pectin lyase-likesearch PF00544: Pectate lyasesearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A (P11073) pectin catabolic processsearch pathogenesissearch pectate lyase activitysearch metal ion bindingsearch lyase activitysearch extracellular regionsearch

Chain InterPro annotation
A Pectate lyase/Amb allergensearch Pectin lyase fold/virulence factorsearch Pectin lyase foldsearch