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Structure of IDP00795

The Crystal Structure of a Dihydroorotase from Staphylococcus aureus

Edit deposit information
CSGID target
IDP00795 
PDB Id
3GRI (NCBI MMDB
Authors
J.S.Brunzelle,Z.Wawrzak,T.Skarina,O.Onopriyenko,A.Savchenko,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Joseph Brunzelle 
Responsible lab
Northwestern University 
Deposition Date
Mar 25, 2009 
Release Date
May 19, 2009 

Annotation

Description
Dihydroorotase (EC 3.5.2.3) catalyzes the third step in pyrimidine biosynthesis, namely, the reversible cyclization of carbamoyl aspartate to form dihydroorotate. In humans, the amidohydrolase activity of dihyroorotate (DHO), which is the reverse of the biosynthetic reaction, is responsible for inactivating the cardioprotective drug, dexrazoxane. DHO is a two-domain structure, one domain is formed by the N and C-terminus (1-55 and 366–422) and a distorted TIM barrel. 
Functional assignment
 

Ligands

Ligand code Name Ligand type
CA
CL CHLORIDE ION
ZN ZINC ION
MSE modified residue

Structure information

Unit cell parameters

Space Group
P 1  
Unit Cell

a=50.22Å, b=55.23Å, c=85.65Å
α=88.33, β=76.56, γ=76.97 
Solvent content
48.78  
Matthews coefficient
2.4  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
30.00-2.00Å (2.05-2.00Å)  
Rall(%)
19.1 
Rwork(%)
18.9 (22.7) 
Rfree(%)
23.7 (28.7) 
Num. observed reflections
57572 (4201) 
Num. Rfree reflections
2936 (207) 
Completeness(%)
97.8 (96.5) 

Model parameters

Num Atoms
6952  
Num Waters
478  
Num Hetatoms
0  
Model mean isotropic B factor
26.700Å2  
RMSD bond length
0.013Å  
RMSD bond angle
1.436°  
Filename uploaded
b8_deposit_idp795.pdb (uploaded on Mar 31, 2009 12:37 PM)  
Inserted
Mar 31, 2009