5bca
From Proteopedia
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|PDB= 5bca |SIZE=350|CAPTION= <scene name='initialview01'>5bca</scene>, resolution 2.2Å | |PDB= 5bca |SIZE=350|CAPTION= <scene name='initialview01'>5bca</scene>, resolution 2.2Å | ||
|SITE= <scene name='pdbsite=CAA:Catalytic+Residues'>CAA</scene>, <scene name='pdbsite=CAB:Catalytic+Residues'>CAB</scene>, <scene name='pdbsite=CAC:Catalytic+Residues'>CAC</scene> and <scene name='pdbsite=CAD:Catalytic+Residues'>CAD</scene> | |SITE= <scene name='pdbsite=CAA:Catalytic+Residues'>CAA</scene>, <scene name='pdbsite=CAB:Catalytic+Residues'>CAB</scene>, <scene name='pdbsite=CAC:Catalytic+Residues'>CAC</scene> and <scene name='pdbsite=CAD:Catalytic+Residues'>CAD</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Beta-amylase Beta-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.2 3.2.1.2] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-amylase Beta-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.2 3.2.1.2] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5bca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bca OCA], [http://www.ebi.ac.uk/pdbsum/5bca PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=5bca RCSB]</span> | ||
}} | }} | ||
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[[Category: Oyama, T.]] | [[Category: Oyama, T.]] | ||
[[Category: Takasaki, Y.]] | [[Category: Takasaki, Y.]] | ||
| - | [[Category: CA]] | ||
[[Category: beta-amylase]] | [[Category: beta-amylase]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: raw-starch binding domain]] | [[Category: raw-starch binding domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:40:54 2008'' |
Revision as of 02:40, 31 March 2008
| |||||||
| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , and | ||||||
| Ligands: | |||||||
| Activity: | Beta-amylase, with EC number 3.2.1.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BETA-AMYLASE FROM BACILLUS CEREUS VAR. MYCOIDES
Overview
The crystal structure of beta-amylase from Bacillus cereus var. mycoides was determined by the multiple isomorphous replacement method. The structure was refined to a final R-factor of 0.186 for 102,807 independent reflections with F/sigma(F) > or = 2.0 at 2.2 A resolution with root-mean-square deviations from ideality in bond lengths, and bond angles of 0.014 A and 3.00 degrees, respectively. The asymmetric unit comprises four molecules exhibiting a dimer-of-dimers structure. The enzyme, however, acts as a monomer in solution. The beta-amylase molecule folds into three domains; the first one is the N-terminal catalytic domain with a (beta/alpha)8 barrel, the second one is the excursion part from the first one, and the third one is the C-terminal domain with two almost anti-parallel beta-sheets. The active site cleft, including two putative catalytic residues (Glu172 and Glu367), is located on the carboxyl side of the central beta-sheet in the (beta/alpha)8 barrel, as in most amylases. The active site structure of the enzyme resembles that of soybean beta-amylase with slight differences. One calcium ion is bound per molecule far from the active site. The C-terminal domain has a fold similar to the raw starch binding domains of cyclodextrin glycosyltransferase and glucoamylase.
About this Structure
5BCA is a Single protein structure of sequence from Bacillus cereus. Full crystallographic information is available from OCA.
Reference
Crystal structure of beta-amylase from Bacillus cereus var. mycoides at 2.2 A resolution., Oyama T, Kusunoki M, Kishimoto Y, Takasaki Y, Nitta Y, J Biochem. 1999 Jun;125(6):1120-30. PMID:10348915
Page seeded by OCA on Mon Mar 31 05:40:54 2008
