Zinc in PDB 3ur3: Structure of the CMR2 Subunit of the Crispr Rna Silencing Complex

The structure of Structure of the CMR2 Subunit of the Crispr Rna Silencing Complex, PDB code: 3ur3 was solved by A.I.Cocozaki, N.F.Ramia, Y.Shao, C.R.Hale, R.M.Terns, M.P.Terns, H.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.68 / 2.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	70.635, 80.211, 143.934, 90.00, 90.00, 90.00
R / Rfree (%)	21.8 / 27.3

The structure of Structure of the CMR2 Subunit of the Crispr Rna Silencing Complex also contains other interesting chemical elements:

Calcium

(Ca)

2 atoms

The binding sites of Zinc atom in the Structure of the CMR2 Subunit of the Crispr Rna Silencing Complex (pdb code 3ur3). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Structure of the CMR2 Subunit of the Crispr Rna Silencing Complex, PDB code: 3ur3:

Zinc binding site 1 out of 1 in the Structure of the CMR2 Subunit of the Crispr Rna Silencing Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the CMR2 Subunit of the Crispr Rna Silencing Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn903 b:97.0 occ:1.00 SG C:CYS478 2.3 86.7 1.0 SG C:CYS481 2.4 82.7 1.0 SG C:CYS448 2.4 92.1 1.0 SG C:CYS451 2.4 92.5 1.0 CB C:CYS478 3.2 81.6 1.0 CB C:CYS481 3.3 80.5 1.0 ND2 C:ASN454 3.6 0.6 1.0 CB C:CYS451 3.6 0.7 1.0 N C:CYS478 3.9 85.1 1.0 CB C:CYS448 3.9 0.9 1.0 N C:CYS451 3.9 0.8 1.0 N C:CYS481 4.1 70.8 1.0 CA C:CYS478 4.1 82.5 1.0 CA C:CYS481 4.3 72.9 1.0 CA C:CYS451 4.3 0.4 1.0 N C:GLY452 4.6 0.3 1.0 C C:CYS478 4.7 75.8 1.0 CB C:VAL450 4.7 93.9 1.0 O C:CYS478 4.8 76.2 1.0 CG C:ASN454 4.9 0.1 1.0

A.I.Cocozaki, N.F.Ramia, Y.Shao, C.R.Hale, R.M.Terns, M.P.Terns, H.Li. Structure of the CMR2 Subunit of the Crispr-Cas Rna Silencing Complex. Structure V. 20 545 2012.
ISSN: ISSN 0969-2126
PubMed: 22405013
DOI: 10.1016/J.STR.2012.01.018