2ntb Summary

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Crystal structure of pectin methylesterase in complex with hexasaccharide V

The structure was published by Fries, M., Ihrig, J., Brocklehurst, K., Shevchik, V.E., and Pickersgill, R.W., in 2007 in a paper entitled "Molecular basis of the activity of the phytopathogen pectin methylesterase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 2006.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of Pectinesterase A.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 Pectinesterase A P0C1A9 (25-366) (PMEA_DICD3)search Dickeya dadantii 3937search 100% 342 100%
B Pectinesterase A P0C1A9 (25-366) (PMEA_DICD3)search Dickeya dadantii 3937search 100% 342 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P0C1A9 (25 - 366) Pectinesterase A Dickeya dadantii 3937

Chain Structural classification (CATH) Sequence family (Pfam)
A, B (P0C1A9) Single-stranded right-handed beta-helix, Pectin lyase-likesearch PF01095: Pectinesterasesearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A, B (P0C1A9) aspartyl esterase activitysearch pectinesterase activitysearch hydrolase activitysearch cell wall organizationsearch cell wall modificationsearch pectin catabolic processsearch extracellular regionsearch cell wallsearch

Chain InterPro annotation
A, B Pectinesterase, catalyticsearch Pectin lyase fold/virulence factorsearch Pectin lyase foldsearch Pectinesterase, active sitesearch