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Structure of IDP02454

Crystal structure of Transketolase from Bacillus anthracis

Edit deposit information
CSGID target
IDP02454 
PDB Id
3HYL (NCBI MMDB
Authors
N.Maltseva,Y.Kim,K.Kwon,A.Joachimiak,W.F.Anderson 
Responsible person
Natalia Maltseva 
Responsible lab
Argonne National Laboratory 
Deposition Date
Jun 22, 2009 
Release Date
Jun 30, 2009 

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 was determined by SAD to 2.16A. 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
CL CHLORIDE ION
GOL
MG MAGNESIUM ION
PEG
SO4
MSE modified residue
FMT

Structure information

Unit cell parameters

Space Group
C 1 2 1  
Unit Cell

a=138.80Å, b=70.97Å, c=145.79Å
α=90.00, β=117.35, γ=90.00 
Solvent content
41.14  
Matthews coefficient
2.09  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
36.35-2.16Å (2.19-2.16Å)  
Rall(%)
17.8 
Rwork(%)
17.6 (24.4) 
Rfree(%)
23.0 (27.4) 
Num. observed reflections
71043 (2570) 
Num. Rfree reflections
3594 (123) 
Completeness(%)
99.4 (92.0) 

Model parameters

Num Atoms
10868  
Num Waters
604  
Num Hetatoms
0  
Model mean isotropic B factor
50.760Å2  
RMSD bond length
0.014Å  
RMSD bond angle
1.532°  
RMSD dihedral angle
19.47°
 
Filename uploaded
dep1w.pdb (uploaded on Jun 23, 2009 9:29 AM)  
Inserted
Jun 23, 2009