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Structure of IDP01892

1.95 Angstrom Crystal Structure of Complex of Hypoxantine-GuaninePhosphoribosyltransferase from Bacillus anthracis with2-(N-morpholino)ethanesulfonic acid (MES)

Edit deposit information
CSGID target
IDP01892 
PDB Id
3HVU (NCBI MMDB
Authors
G.Minasov,A.Halavaty,L.Shuvalova,I.Dubrovska,J.Winsor,L.Papazisi,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
George Minasov 
Responsible lab
Northwestern University 
Deposition Date
Jun 16, 2009 
Release Date
Jun 23, 2009 

Annotation

Description
The purine nucleotides play a key role in synthesis of DNA, RNA and ATP supply. Living organisms can produce purine nucleotides de novo or via the salvage pathway. Two pathways are inter-related, share alpha-D-phosphoribosyl-1-pyrophosphate (PRPP) as a common substrate and may impose regulation on each other. Many pathogenic organisms are deficient in de novo synthesis of the purine nucleotides, and therefore must rely on the salvage pathway. The key enzyme in the latter pathway is a hypoxanthine-guanine phosphoribosyltransferase (HGPRT, E.C. 2.4.2.8), which catalyzes a reversible transfer of the 5-phosphoribosyl group from PRPP to the N9 atom of either hypoxanthine or guanine to form inosine 5'-monophosphate (IMP) or guanosine 5'-monophosphate (GMP), respectively. It is of scientific and medical interest to understand the mechanism of the HGPRT-catalyzed reaction, because it will help to develop inhibition strategies of the enzyme, and hence create therapeutic agents for treatment of diseases caused by human pathogens. 
Functional assignment
Transferase 

Ligands

Ligand code Name Ligand type
NA Sodium ion crystallization
175 3,5-dihydro-5-methylidene-4h-imidazol-4-on

Structure information

Unit cell parameters

Space Group
P 1 21 1  
Unit Cell

a=52.71Å, b=93.38Å, c=94.90Å
α=90.00, β=90.03, γ=90.00 
Solvent content
51.6  
Matthews coefficient
2.54  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
29.96-1.95Å (2.00-1.95Å)  
Rall(%)
19.4 
Rwork(%)
19.2 (27.3) 
Rfree(%)
23.2 (29.3) 
Num. observed reflections
65670 (4574) 
Num. Rfree reflections
3349 (252) 
Completeness(%)
98.1 (94.2) 

Model parameters

Num Atoms
6108  
Num Waters
498  
Num Hetatoms
554  
Model mean isotropic B factor
22.880Å2  
RMSD bond length
0.012Å  
RMSD bond angle
1.644°  
Filename uploaded
3HVU.pdb (uploaded on Oct 07, 2010 5:51 PM)  
Inserted
Jun 25, 2009