Magnesium in PDB 6tgv: Crystal Structure of Mycobacterium Smegmatis Coabc in Complex with Ctp and Fmn

The structure of Crystal Structure of Mycobacterium Smegmatis Coabc in Complex with Ctp and Fmn, PDB code: 6tgv was solved by V.Mendes, M.Blaszczyk, O.Bryant, J.Cory-Wright, T.L.Blundell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	62.67 / 2.50
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	195.132, 195.132, 373.725, 90.00, 90.00, 120.00
R / Rfree (%)	20.4 / 24.5

The binding sites of Magnesium atom in the Crystal Structure of Mycobacterium Smegmatis Coabc in Complex with Ctp and Fmn (pdb code 6tgv). 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 Mycobacterium Smegmatis Coabc in Complex with Ctp and Fmn, PDB code: 6tgv:

Magnesium binding site 1 out of 1 in the Crystal Structure of Mycobacterium Smegmatis Coabc in Complex with Ctp and Fmn


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 Mycobacterium Smegmatis Coabc in Complex with Ctp and Fmn within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg505 b:0.2 occ:1.00 O1A A:CTP501 2.3 0.6 1.0 OD2 A:ASP281 2.4 0.7 1.0 CG A:ASP281 3.1 0.8 1.0 O2G A:CTP501 3.1 0.7 1.0 OD1 A:ASP281 3.3 0.5 1.0 PA A:CTP501 3.5 0.0 1.0 O2A A:CTP501 3.6 0.6 1.0 O2B A:CTP501 4.3 0.9 1.0 CB A:ASP281 4.3 0.4 1.0 PG A:CTP501 4.4 0.2 1.0 O3B A:CTP501 4.5 0.3 1.0 C5 A:CTP501 4.6 0.2 1.0 O5' A:CTP501 4.6 0.7 1.0 O3A A:CTP501 4.7 0.0 1.0 PB A:CTP501 4.8 0.2 1.0 C6 A:CTP501 5.0 0.0 1.0

V.Mendes, S.Green, J.C.Evans, J.Hess, M.Blaszczyk, C.Spry, O.Bryant, J.Cory-Wright, D.S.Chan, P.H.M.Torres, Z.Wang, S.O'neill, S.Damerow, J.Post, T.Bayliss, S.L.Lynch, A.G.Coyne, P.C.Ray, C.Abell, K.Rhee, H.I.M.Boshoff, C.E.Barry, V.Mizrahi, P.G.Wyatt, T.L.Blundell. Inhibiting Mycobacterium Tuberculosis Coabc By Targeting A New Cryptic Allosteric Site. To Be Published.