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Structure of IDP90790

Isopropylmalate isomerase small subunit from Campylobacter jejuni.

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CSGID target
IDP90790 
PDB Id
3Q3W (NCBI MMDB) 
Authors
'J.Osipiuk,M.Gu,L.Papazisi,W.F.Anderson,A.Joachimiak,Center For Structural Genomics Of Infectious Diseases (Csgid)' 
Responsible person
Jerzy Osipiuk 
Responsible lab
Argonne National Laboratory 
Deposition Date
Dec 22, 2010 
Release Date
Jan 26, 2011 

Annotation

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Description
Isopropylmalate isomerase (IPMI) catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate in leucine biosynthesis. IPMI exists as a complex of two subunits: the large (LeuC) and the small (LeuD) subunit. The absence of the leucine biosynthesis pathway in humans makes the enzymes of this pathway in pathogenic bacteria such as Mycobacterium tuberculosis potential candidates for developing novel antibacterial drugs.  
Functional assignment
Isomerase 

Ligands

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

Structure information

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Unit cell parameters

Space Group
P 21 21 2  
Unit Cell

a=74.50Å, b=151.94Å, c=32.72Å
α=90.00, β=90.00, γ=90.00 
Solvent content
38.1  
Matthews coefficient
1.99  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
42.00-1.88Å (1.93-1.88Å)  
Rall(%)
18.9 
Rwork(%)
18.7 (30.3) 
Rfree(%)
23.2 (34.2) 
Num. observed reflections
28862 (1849) 
Num. Rfree reflections
1471 (96) 
Completeness(%)
92.9 (81.1) 

Model parameters

Num Atoms
3243  
Num Waters
213  
Num Hetatoms
0  
Model mean isotropic B factor
14.890Å2  
RMSD bond length
0.019Å  
RMSD bond angle
1.599°  
Filename uploaded
idp90790.pdb (uploaded on Dec 22, 2010 2:08 PM)  
Inserted
Dec 22, 2010