Annotation

Description

Cytosol aminopeptidases belong to the peptidase M17 family and are involved in the processing and regular turnover of intracellular proteins. Aminopeptidases catalyze the removal of the unsubstituted N-terminal amino acid from various proteins and small peptides. They are widely distributed among prokaryotes and eukaryotes and typically are hexameric enzymes. In known cases each of six subunits contains two Zn2+/Mn 2+ ions in the active site, which are fundamental for catalytic activity and exhibit different metal ion exchange kinetics. In the apo form structure subunits that form the hexamer contain two domains with mixed α/β structure that are linked by a long α-helix. The loop (residues 258-269) which forms the part of the active site is disordered and there are no Zn2+/Mn 2+ ions found in the present structure. 

Functional assignment

 

Structure information

Unit cell parameters

Space Group

P 63 2 2  

Unit Cell

a=161.48Å, b=161.48Å, c=105.27Å
α=90.00, β=90.00, γ=120.00 

Solvent content

66.5  

Matthews coefficient

3.67  

Refinement

Data for the highest resolution shell is in parentheses.

Resolution range

50.00-2.70Å (2.77-2.70Å)  

R_all(%)

16.7 

R_work(%)

16.5 (22.1) 

R_free(%)

21.0 (33.6) 

Num. observed reflections

22659 (1608) 

Num. R_free reflections

1155 (94) 

Completeness(%)

99.7 (98.2) 

Model parameters

Num Atoms

4014  

Num Waters

366  

Num Hetatoms

0  

Model mean isotropic B factor

52.560Ų  

RMSD bond length

0.011Å  

RMSD bond angle

1.339°  

Filename uploaded

dep.pdb (uploaded on Oct 26, 2010 1:24 PM)  

Inserted

Oct 26, 2010