To see full content of that page you need the activeISee plugin.
Get the latest version from here.

Structure of IDP01139

Xaa-Pro dipeptidase from Bacillus anthracis.

Edit deposit information
CSGID target
IDP01139 
PDB Id
3Q6D (NCBI MMDB
Authors
J.Osipiuk,M.Makowska-Grzyska,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 31, 2010 
Release Date
Feb 02, 2011 

Annotation

Description
Xaa-Pro dipeptidase, also known as prolidase, hydrolizes dipeptides having proline as the second residue. Enzymes of this type have been found in mammals, bacteria, and archeon Pyrococcus horikoshii. In humans, prolidase is involved in the final stage of the degradation of endogenous and dietary proteins, and is particularly important in collagen catabolism. Mutations in the gene encoding for human prolidase cause an autosomal recessive disorder characterized by skin lesions, mental retardation, and recurrent infections. The physiological role of the enzyme in bacteria is not established. In general, proline-specific peptidases participate with other peptidases in the terminal degradation of intracellular proteins, and may function in the recycling of proline.  
Functional assignment
Peptidase 

Ligands

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

Structure information

Unit cell parameters

Space Group
P 21 21 21  
Unit Cell

a=59.50Å, b=107.91Å, c=252.85Å
α=90.00, β=90.00, γ=90.00 
Solvent content
52.81  
Matthews coefficient
2.61  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
45.90-1.97Å (2.02-1.97Å)  
Rall(%)
19.8 
Rwork(%)
19.6 (27.4) 
Rfree(%)
24.7 (32.6) 
Num. observed reflections
113552 (7438) 
Num. Rfree reflections
5677 (382) 
Completeness(%)
97.3 (87.7) 

Model parameters

Num Atoms
11198  
Num Waters
653  
Num Hetatoms
663  
Model mean isotropic B factor
19.040Å2  
RMSD bond length
0.018Å  
RMSD bond angle
1.618°  
Filename uploaded
rcsb063250.pdb (uploaded on Jan 11, 2011 12:55 PM)  
Inserted
Jan 11, 2011