1jgi Summary


Crystal Structure of the Active Site Mutant Glu328Gln of Amylosucrase from Neisseria polysaccharea in Complex with the Natural Substrate Sucrose

The structure was published by Mirza, O., Skov, L.K., Remaud-Simeon, M., et al., Albenne, C., Monsan, P., and Gajhede, M., in 2001 in a paper entitled "Crystal structures of amylosucrase from Neisseria polysaccharea in complex with D-glucose and the active site mutant Glu328Gln in complex with the natural substrate sucrose." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2001.

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

The PDB entry contains the structure of amylosucrase. This molecule has the UniProt identifier Q9ZEU2 (AMYS_NEIPO)search. The sample contained 628 residues which is 98% of the natural sequence. Out of 628 residues 628 were observed and are deposited in the PDB.

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 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 amylosucrase Q9ZEU2 (13-636) (AMYS_NEIPO)search Neisseria polysacchareasearch 98% 628 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q9ZEU2 (13 - 636) amylosucrase Neisseria polysaccharea

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (Q9ZEU2) alpha-Amylases, C-terminal beta-sheet domainsearch, Amylase, catalytic domainsearch Glycosidasessearch, Oligo-1,6-glucosidase; Domain 2search, Golgi alpha-mannosidase IIsearch PF00128: Alpha amylase, catalytic domainsearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A (Q9ZEU2) catalytic activitysearch transferase activitysearch cation bindingsearch amylosucrase activitysearch transferase activity, transferring glycosyl groupssearch extracellular regionsearch carbohydrate metabolic processsearch

Chain InterPro annotation
A Glycosyl hydrolase, family 13, catalytic domainsearch Glycosyl hydrolase, family 13, all-betasearch Glycoside hydrolase, catalytic domainsearch Glycoside hydrolase, family 13search Glycoside hydrolase superfamilysearch