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Structure of IDP02454

Crystal Structure of Transketolase Complexed with Thiamine Diphosphate from Bacillus anthracis

Edit deposit information
CSGID target
IDP02454 
PDB Id
3M49 (NCBI MMDB
Authors
N.Maltseva,Y.Kim,K.Kwon,W.F.Anderson,A.Joachimiak 
Responsible person
Natalia Maltseva 
Responsible lab
Argonne National Laboratory 
Deposition Date
Mar 10, 2010 
Release Date
Apr 07, 2010 

Annotation

Description
Transketolase (tkt-2) is an evolutionarily conserved enzyme which catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. The structure complexed with thiamine pyrophosphate was determined by SAD to 2.0 A. The protein forms homodimer where each molecule consists of three aba sandwich domains of different size.  
Functional assignment
 

Ligands

Ligand code Name Ligand type
PG5 crystallization
TDP thiamin diphosphate biological
SO4
FMT
GOL
ACY
PEG
TRS Tris(hydroxymethyl)aminomethane
MG
BTB 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol
MSE modified residue

Structure information

Unit cell parameters

Space Group
P 21 21 21  
Unit Cell

a=83.33Å, b=132.09Å, c=137.32Å
α=90.00, β=90.00, γ=90.00 
Solvent content
50.32  
Matthews coefficient
2.48  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
31.73-2.00Å (2.07-2.00Å)  
Rall(%)
13.9 
Rwork(%)
13.7 (15.0) 
Rfree(%)
17.2 (19.7) 
Num. observed reflections
107161 (10013) 
Num. Rfree reflections
5347 (501) 
Completeness(%)
99.2 (99.0) 

Model parameters

Num Atoms
11757  
Num Waters
1130  
Num Hetatoms
0  
Model mean isotropic B factor
23.370Å2  
RMSD bond length
0.012Å  
RMSD bond angle
1.278°  
RMSD dihedral angle
16.85°
 
Filename uploaded
dep1wa.pdb (uploaded on Mar 10, 2010 4:46 PM)  
Inserted
Oct 27, 2009