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Structure of IDP02500

GBAA_1210 protein, a putative adenylate cyclase, from Bacillus anthracis.

Edit deposit information
CSGID target
IDP02500 
PDB Id
3SY3 (NCBI MMDB
Authors
'J.Osipiuk,M.Gu,K.Kwon,W.F.Anderson,A.Joachimiak,Center For Structural Genomics Of Infectious Diseases (Csgid)' 
Responsible person
Jerzy Osipiuk 
Responsible lab
Argonne National Laboratory 
Deposition Date
Jul 15, 2011 
Release Date
Jul 27, 2011 

Annotation

Description
Cyclic adenosine monophosphate (cAMP, cyclic AMP or 3'-5'-cyclic adenosine monophosphate) is an important signaling molecule in virtually all prokaryotic and eukaryotic cells. It activates diverse bacterial cAMP receptor proteins such as transcription factors and protein kinases. cAMP is derived from adenosine triphosphate (ATP) in reaction catalyzed by adenylate cyclase (AC). There are six distinct non-homologous classes of ACs. The majority of enzymes belong to class III which converts ATP to cAMP in a catalytic center formed by an interface of protein homodimers. GBAA_1210 protein monomer structure has the same fold as class IV AC from Yersinia pestis (3N10 deposit in PDB); however, it displays a different dimer organization at least inside crystals. The Y. pestis AC monomer forms an antiparallel eight-stranded barrel which binds ligands inside the barrel.  
Functional assignment
 

Ligands

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

Structure information

Unit cell parameters

Space Group
P 1 21 1  
Unit Cell

a=67.32Å, b=86.00Å, c=76.51Å
α=90.00, β=102.12, γ=90.00 
Solvent content
 
Matthews coefficient
 

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
37.28-2.14Å (2.20-2.14Å)  
Rall(%)
19.9 
Rwork(%)
19.6 (28.4) 
Rfree(%)
24.8 (33.7) 
Num. observed reflections
46743 (3169) 
Num. Rfree reflections
2337 (139) 
Completeness(%)
99.1 (91.6) 

Model parameters

Num Atoms
5947  
Num Waters
173  
Num Hetatoms
0  
Model mean isotropic B factor
36.750Å2  
RMSD bond length
0.018Å  
RMSD bond angle
1.590°  
Filename uploaded
idp02500.pdb (uploaded on Jul 15, 2011 3:17 PM)  
Inserted
Jul 15, 2011