1pp4 Summary


The crystal structure of rhamnogalacturonan acetylesterase in space group P3121

The structure was published by Molgaard, A. and Larsen, S., in 2004 in a paper entitled "Crystal packing in two pH-dependent crystal forms of rhamnogalacturonan acetylesterase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 2003.

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

This PDB entry contains multiple copies of the structure of Rhamnogalacturonan acetylesterase.

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 Rhamnogalacturonan acetylesterase Q00017 (18-250) (RHA1_ASPAC)search Aspergillus aculeatussearch 100% 233 100%
B Rhamnogalacturonan acetylesterase Q00017 (18-250) (RHA1_ASPAC)search Aspergillus aculeatussearch 100% 233 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q00017 (18 - 250) Rhamnogalacturonan acetylesterase Aspergillus aculeatus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (Q00017) Rhamnogalacturonan acetylesterasesearch Rossmann foldsearch PF00657: GDSL-like Lipase/Acylhydrolasesearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (Q00017) hydrolase activitysearch hydrolase activity, acting on ester bondssearch lipid metabolic processsearch

Chain InterPro annotation
A, B Lipase, GDSLsearch SGNH hydrolase-type esterase domainsearch