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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 crystallization
PGE crystallization
CL CHLORIDE ION 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