1bvz Summary

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ALPHA-AMYLASE II (TVAII) FROM THERMOACTINOMYCES VULGARIS R-47

The structure was published by Kamitori, S., Kondo, S., Okuyama, K., et al., Shimura, Y., Tonozuka, T., and Sakano, Y., in 1999 in a paper entitled "Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 A resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.6 Å and deposited in 1998.

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

This PDB entry contains multiple copies of the structure of PROTEIN (ALPHA-AMYLASE II).

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 PROTEIN (ALPHA-AMYLASE II) Q08751 (1-585) (NEPU2_THEVU)search Thermoactinomyces vulgarissearch 100% 585 100%
B PROTEIN (ALPHA-AMYLASE II) Q08751 (1-585) (NEPU2_THEVU)search Thermoactinomyces vulgarissearch 100% 585 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q08751 (1 - 585) PROTEIN (ALPHA-AMYLASE II) Thermoactinomyces vulgaris

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (Q08751) E-set domains of sugar-utilizing enzymessearch, alpha-Amylases, C-terminal beta-sheet domainsearch, Amylase, catalytic domainsearch Immunoglobulinssearch, Glycosidasessearch, Golgi alpha-mannosidase IIsearch PF00128: Alpha amylase, catalytic domainsearch, PF02806: Alpha amylase, C-terminal all-beta domainsearch, PF02903: Alpha amylase, N-terminal ig-like domainsearch

Chain ID Biological process (GO) Molecular function (GO)
A, B (Q08751) carbohydrate metabolic processsearch metabolic processsearch catalytic activitysearch cation bindingsearch hydrolase activity, acting on glycosyl bondssearch metal ion bindingsearch neopullulanase activitysearch hydrolase activitysearch hydrolase activity, hydrolyzing O-glycosyl compoundssearch

Chain InterPro annotation
A, B Glycoside hydrolase, family 13, N-terminal Ig-like domainsearch Glycosyl hydrolase, family 13, catalytic domainsearch Alpha-amylase, C-terminal all betasearch Glycosyl hydrolase, family 13, subfamily, catalytic domainsearch Glycosyl hydrolase, family 13, all-betasearch Glycoside hydrolase, catalytic domainsearch Immunoglobulin-like foldsearch Immunoglobulin E-setsearch Glycoside hydrolase, family 13search Glycoside hydrolase, superfamilysearch