Magnesium in PDB 4cmp: Crystal Structure of S. Pyogenes CAS9

The structure of Crystal Structure of S. Pyogenes CAS9, PDB code: 4cmp was solved by M.Jinek, F.Jiang, D.W.Taylor, S.H.Sternberg, E.Kaya, E.Ma, C.Anders, M.Hauer, K.Zhou, S.Lin, M.Kaplan, A.T.Iavarone, E.Charpentier, E.Nogales, J.A.Doudna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.481 / 2.62
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	159.780, 209.620, 91.260, 90.00, 90.00, 90.00
R / Rfree (%)	25.23 / 28.58

The binding sites of Magnesium atom in the Crystal Structure of S. Pyogenes CAS9 (pdb code 4cmp). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of S. Pyogenes CAS9, PDB code: 4cmp:

Magnesium binding site 1 out of 1 in the Crystal Structure of S. Pyogenes CAS9


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of S. Pyogenes CAS9 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg2367 b:54.1 occ:1.00 O B:HOH2004 2.2 51.2 1.0 OD2 B:ASP986 2.2 45.8 1.0 OD1 B:ASP10 3.0 39.8 1.0 OD2 B:ASP10 3.0 39.9 1.0 CG B:ASP986 3.1 32.1 1.0 HB3 B:ASP986 3.4 35.6 1.0 CG B:ASP10 3.4 37.9 1.0 O B:HOH2003 3.5 56.6 1.0 OE1 B:GLU762 3.6 64.2 1.0 CB B:ASP986 3.7 29.7 1.0 HZ2 B:LYS974 3.9 47.0 1.0 HB2 B:ASP986 3.9 35.6 1.0 HZ1 B:LYS974 3.9 47.0 1.0 OD1 B:ASP986 4.0 29.9 1.0 NZ B:LYS974 4.3 39.1 1.0 HZ3 B:LYS974 4.5 47.0 1.0 CD B:GLU762 4.6 63.9 1.0 OE2 B:GLU762 4.8 67.4 1.0 CB B:ASP10 4.9 25.0 1.0 HD22 B:ASN990 4.9 30.4 1.0 HD1 B:HIS983 4.9 37.4 1.0 HA B:HIS983 5.0 35.2 1.0

M.Jinek, F.Jiang, D.W.Taylor, S.H.Sternberg, E.Kaya, E.Ma, C.Anders, M.Hauer, K.Zhou, S.Lin, M.Kaplan, A.T.Iavarone, E.Charpentier, E.Nogales, J.A.Doudna. Structures of CAS9 Endonucleases Reveal Rna-Mediated Conformational Activation. Science V. 343 47997 2014.
ISSN: ISSN 0036-8075
PubMed: 24505130
DOI: 10.1126/SCIENCE.1247997