Arsenic in PDB 3ucy: Structure of MG2+ Bound N-Terminal Domain of Calmodulin in the Presence of ZN2+

The structure of Structure of MG2+ Bound N-Terminal Domain of Calmodulin in the Presence of ZN2+, PDB code: 3ucy was solved by F.T.Senguen, Z.Grabarek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.73 / 1.80
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	35.298, 35.298, 142.937, 90.00, 90.00, 90.00
R / Rfree (%)	20.1 / 22.8

The structure of Structure of MG2+ Bound N-Terminal Domain of Calmodulin in the Presence of ZN2+ also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Zinc	(Zn)	2 atoms
Sodium	(Na)	1 atom

The binding sites of Arsenic atom in the Structure of MG2+ Bound N-Terminal Domain of Calmodulin in the Presence of ZN2+ (pdb code 3ucy). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total only one binding site of Arsenic was determined in the Structure of MG2+ Bound N-Terminal Domain of Calmodulin in the Presence of ZN2+, PDB code: 3ucy:

Arsenic binding site 1 out of 1 in the Structure of MG2+ Bound N-Terminal Domain of Calmodulin in the Presence of ZN2+


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Structure of MG2+ Bound N-Terminal Domain of Calmodulin in the Presence of ZN2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:As200 b:30.0 occ:1.00 AS A:CAC200 0.0 30.0 1.0 O1 A:CAC200 1.7 30.0 1.0 O2 A:CAC200 1.7 30.0 1.0 C2 A:CAC200 1.9 30.0 1.0 C1 A:CAC200 2.0 30.0 1.0 ZN A:ZN102 3.2 29.8 1.0 OG1 A:THR26 3.3 35.5 1.0 NA A:NA100 3.8 28.2 1.0 O A:HOH301 4.2 30.0 1.0 O A:THR26 4.4 28.3 1.0 CB A:THR26 4.5 30.6 1.0 OD2 A:ASP24 4.6 32.5 1.0 OD2 A:ASP22 4.6 30.3 1.0 OD1 A:ASP24 4.7 29.5 1.0 OG1 A:THR62 4.7 38.5 1.0 C A:THR26 4.7 27.5 1.0 OD1 A:ASP22 4.9 27.9 1.0

F.T.Senguen, Z.Grabarek. X-Ray Structures of Magnesium and Manganese Complexes with the N-Terminal Domain of Calmodulin: Insights Into the Mechanism and Specificity of Metal Ion Binding to An Ef-Hand. Biochemistry V. 51 6182 2012.
ISSN: ISSN 0006-2960
PubMed: 22803592
DOI: 10.1021/BI300698H