1jf5 Summary



The structure was published by Ohtaki, A., Kondo, S., Shimura, Y., Tonozuka, T., Sakano, Y., and Kamitori, S., in 2001 in a paper entitled "Role of Phe286 in the recognition mechanism of cyclomaltooligosaccharides (cyclodextrins) by Thermoactinomyces vulgaris R-47 alpha-amylase 2 (TVAII). X-ray structures of the mutant TVAIIs, F286A and F286Y, and kinetic analyses of the Phe286-replaced mutant TVAIIs" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 3.2 Å and deposited in 2001.

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

This PDB entry contains multiple copies of the structure of ALPHA AMYLASE II.

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 most likely forms homodimers.

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 ALPHA AMYLASE II Q08751 (1-585) (NEPU2_THEVU)search Thermoactinomyces vulgarissearch 100% 585 100%
B 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) 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 Molecular function (GO) Biological process (GO)
A, B (Q08751) catalytic activitysearch hydrolase activity, hydrolyzing O-glycosyl compoundssearch hydrolase activitysearch hydrolase activity, acting on glycosyl bondssearch neopullulanase activitysearch cation bindingsearch metal ion bindingsearch carbohydrate metabolic processsearch metabolic processsearch

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