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

Structure of IDP02095

1.85 Angstrom Resolution Crystal Structure of Transaldolase B (talA) from Francisella tularensis.

Edit deposit information
CSGID target
IDP02095 
PDB Id
3IGX (NCBI MMDB
Authors
G.Minasov,Z.Wawrzak,T.Skarina,E.Gordon,S.N.Peterson,A.Savchenko,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
George Minasov 
Responsible lab
Northwestern University 
Deposition Date
Jul 29, 2009 
Release Date
Aug 11, 2009 

Annotation

Description
Transaldolase B is an enzyme of the Class I aldose family and catalyzes the reversible transer of a dihydroxyacetone moiety, derived from fructose-6-phosphate, to erythrose-4-phosphate yielding sedohepptulose-7-phosphate. This reaction is a part of the pentose phosphate pathway, an anabolic pathway that utilizes the 6 carbons of glucose to generate 5 carbon sugars and reducing equivalents. A common feature of the members of this enzyme family is the formation of a covalent intermediate (Schiff base) between an active site lysine residue and the substrate during catalysis. The enzyme is of considerable interest as a catalyst in stereospecific organic synthesis. It is also a target for drug design, because Transaldolase (TAL) is involved in oxidative stress and apoptosis, in multiple sclerosis, and its deficiency leads to severe symptoms in human.  
Functional assignment
Transaldolase B 

Ligands

Ligand code Name Ligand type
PO4 PHOSPHATE ION
MSE modified residue

Structure information

Unit cell parameters

Space Group
P 21 21 21  
Unit Cell

a=56.49Å, b=75.86Å, c=164.77Å
α=90.00, β=90.00, γ=90.00 
Solvent content
49.43  
Matthews coefficient
2.43  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
29.41-1.85Å (1.90-1.85Å)  
Rall(%)
15.1 
Rwork(%)
15.0 (20.4) 
Rfree(%)
18.6 (26.2) 
Num. observed reflections
61062 (4285) 
Num. Rfree reflections
3114 (212) 
Completeness(%)
99.6 (96.0) 

Model parameters

Num Atoms
5142  
Num Waters
847  
Num Hetatoms
979  
Model mean isotropic B factor
12.650Å2  
RMSD bond length
0.011Å  
RMSD bond angle
1.290°  
Filename uploaded
validate-2.pdb (uploaded on Jul 29, 2009 11:44 AM)  
Inserted
Jul 29, 2009