To see full content of that page you need the activeISee plugin.
Get the latest version from here.

Structure of IDP00968

1.4 Angstrom Resolution Crystal Structure of Putative alpha Amylase from Salmonella typhimurium.

Edit deposit information
CSGID target
IDP00968 
PDB Id
3M07 (NCBI MMDB
Authors
'G.Minasov,L.Shuvalova,I.Dubrovska,J.Winsor,L.Papazisi,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid)' 
Responsible person
George Minasov 
Responsible lab
Northwestern University 
Deposition Date
Mar 02, 2010 
Release Date
Mar 16, 2010 

Annotation

Description
Alpha-Amylase is an enzyme that hydrolyses alpha-bonds of large alpha-linked polysaccharides such as starch and glycogen, yielding glucose and maltose. Alpha-Amylase is the major form of amylase found in humans and other mammals. The alpha-amylases are calcium metalloenzymes, completely unable to function in the absence of calcium. By acting at random locations along the starch chain, α-amylase breaks down long-chain carbohydrates, ultimately yielding maltotriose and maltose from amylose, or maltose, glucose and "limit dextrin" from amylopectin. Because it can act anywhere on the substrate, α-amylase tends to be faster-acting than β-amylase. In animals, it is a major digestive enzyme and its optimum pH is 6.7-7.0. Alpha-amylase is used in ethanol production to break starches in grains into fermentable sugars. An alpha-amylase called "Termamyl", sourced from Bacillus licheniformis, is also used in some detergents, especially dishwashing and de-starching detergents.  
Functional assignment
Amylase, hydrolysis of long-chain carbohydrates (strach) 

Ligands

Ligand code Name Ligand type
BTB 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol crystallization
MG magnesium crystallization
PGE crystallization
CL chloride crystallization
175 3,5-dihydro-5-methylidene-4h-imidazol-4-on

Structure information

Unit cell parameters

Space Group
C 1 2 1  
Unit Cell

a=174.05Å, b=51.53Å, c=57.01Å
α=90.00, β=101.18, γ=90.00 
Solvent content
32.73  
Matthews coefficient
1.83  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
29.79-1.40Å (1.44-1.40Å)  
Rall(%)
14.9 
Rwork(%)
14.8 (21.9) 
Rfree(%)
17.3 (24.9) 
Num. observed reflections
97181 (6960) 
Num. Rfree reflections
4859 (361) 
Completeness(%)
99.5 (96.9) 

Model parameters

Num Atoms
4963  
Num Waters
616  
Num Hetatoms
721  
Model mean isotropic B factor
17.270Å2  
RMSD bond length
0.013Å  
RMSD bond angle
1.448°  
Filename uploaded
rcsb057942.pdb (uploaded on Mar 06, 2010 10:29 AM)  
Inserted
Mar 06, 2010