1ac0 Summary

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GLUCOAMYLASE, GRANULAR STARCH-BINDING DOMAIN COMPLEX WITH CYCLODEXTRIN, NMR, MINIMIZED AVERAGE STRUCTURE

The structure was published by Sorimachi, K., Le Gal-Coeffet, M.F., Williamson, G., Archer, D.B., and Williamson, M.P., in 1997 in a paper entitled "Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to beta-cyclodextrin." (abstract).

The structure was determined using NMR spectroscopy and deposited in 1997.

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

The PDB entry contains the structure of GLUCOAMYLASE. This molecule has the UniProt identifier P69328 (AMYG_ASPNG)search. The sample contained 108 residues which is < 90% of the natural sequence. Out of 108 residues 108 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 GLUCOAMYLASE P69328 (533-640) (AMYG_ASPNG)search Aspergillus nigersearch < 90% 108 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P69328 (533 - 640) GLUCOAMYLASE Aspergillus niger

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A Starch-binding domainsearch Immunoglobulinssearch Starch binding domainsearch

Chain ID Molecular function (GO)
A (P69328) starch bindingsearch catalytic activitysearch carbohydrate bindingsearch

Chain InterPro annotation
A Carbohydrate binding module family 20search Immunoglobulin-like foldsearch Carbohydrate-binding-like foldsearch Glycoside hydrolase, family 13search