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Structure of IDP90544

Crystal Structure of Dihydrofolate Reductase from Yersinia pestis

Edit deposit information
CSGID target
IDP90544 
PDB Id
3Q1H (NCBI MMDB
Authors
N.Maltseva,Y.Kim,M.Makowska-Grzyska,R.Mulligan,L.Papazisi,W.F.Anderson,A.Joachimiak,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Natalia Maltseva 
Responsible lab
Argonne National Laboratory 
Deposition Date
Dec 17, 2010 
Release Date
Jan 12, 2011 

Annotation

Description
Dihydrofolate reductase is a housekeeping enzyme which is responsible for maintaining the amount of tetrahydrofolate in the cell. It catalyzes the NADPH-linked reduction of 7,8-dihydrofolate to 5,6,7,8- tetrahydrofolate. Tetrahydrofolate is the cofactor used in synthesis of several important metabolites like thymidylate, a building block of DNA. Crystal Structure of Dihydrofolate Reductase from Yersinia pestis was solved at 1.8A resolution. Protein has single domain composed of 4 alpha helices and 8 beta-sheets.  
Functional assignment
 

Ligands

Ligand code Name Ligand type
175 3,5-dihydro-5-methylidene-4h-imidazol-4-on

Structure information

Unit cell parameters

Space Group
C 2 2 21  
Unit Cell

a=60.48Å, b=79.15Å, c=64.69Å
α=90.00, β=90.00, γ=90.00 
Solvent content
41.68  
Matthews coefficient
2.11  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
33.76-1.80Å (1.94-1.80Å)  
Rall(%)
16.7 
Rwork(%)
16.6 (19.4) 
Rfree(%)
20.0 (22.9) 
Num. observed reflections
15223 (2729) 
Num. Rfree reflections
767 (150) 
Completeness(%)
98.9 (95.0) 

Model parameters

Num Atoms
1318  
Num Waters
163  
Num Hetatoms
173  
Model mean isotropic B factor
21.670Å2  
RMSD bond length
0.007Å  
RMSD bond angle
1.057°  
RMSD dihedral angle
12.934°
 
Filename uploaded
dep.pdb (uploaded on Jan 27, 2011 5:18 PM)  
Inserted
Jan 27, 2011