Structure of IDP90544

The high resolution structure of apo form dihydrofolate reductase from Yersinia pestis at 1.55 A

Edit deposit information
CSGID target
IDP90544 
PDB Id
5FDA (NCBI MMDB
Authors
C.Chang,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 15, 2015 
Release Date
Dec 30, 2015 

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 1.55A resolution. Protein has single domain composed of 4 alpha helices and 8 beta-sheets. 
Functional assignment
 

Ligands

Ligand code Name Ligand type
CL CHLORIDE ION crystallization
175 3,5-dihydro-5-methylidene-4h-imidazol-4-on

Structure information

Unit cell parameters

Space Group
C 2 2 21  
Unit Cell

a=60.27Å, b=79.20Å, c=64.32Å
α=90.00, β=90.00, γ=90.00 
Solvent content
 
Matthews coefficient
 

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
47.96-1.55Å (1.62-1.55Å)  
Rall(%)
15.9 
Rwork(%)
15.7 (19.5) 
Rfree(%)
19.4 (27.5) 
Num. observed reflections
23372 (2307) 
Num. Rfree reflections
1168 (120) 
Completeness(%)
97.8 (83.0) 

Model parameters

Num Atoms
1255  
Num Waters
187  
Num Hetatoms
262  
Model mean isotropic B factor
19.050Å2  
RMSD bond length
0.009Å  
RMSD bond angle
0.973°  
RMSD dihedral angle
18.538°
 
Filename uploaded
D_1000216398_model-annotate_P1.pdb (uploaded on Jan 04, 2016 4:16 PM)  
Inserted
Jan 04, 2016