Chlorine in PDB 7bhu: Crystal Structure of MAT2A with Elaborated Fragment 26 Bound in the Allosteric Site

All present enzymatic activity of Crystal Structure of MAT2A with Elaborated Fragment 26 Bound in the Allosteric Site:
2.5.1.6;

The structure of Crystal Structure of MAT2A with Elaborated Fragment 26 Bound in the Allosteric Site, PDB code: 7bhu was solved by M.Schimpl, C.De Fusco, U.Borjesson, T.Cheung, I.Collie, L.Evans, P.Narasimhan, C.Stubbs, M.Vazquez-Chantada, D.J.Wagner, M.Grondine, S.Tentarelli, E.Underwood, A.Argyrou, S.Bagal, E.Chiarparin, G.Robb, J.S.Scott, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	16.38 / 1.15
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	68.24, 94.171, 117.306, 90, 90, 90
R / Rfree (%)	15.3 / 16.9

The binding sites of Chlorine atom in the Crystal Structure of MAT2A with Elaborated Fragment 26 Bound in the Allosteric Site (pdb code 7bhu). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of MAT2A with Elaborated Fragment 26 Bound in the Allosteric Site, PDB code: 7bhu:

Chlorine binding site 1 out of 1 in the Crystal Structure of MAT2A with Elaborated Fragment 26 Bound in the Allosteric Site


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of MAT2A with Elaborated Fragment 26 Bound in the Allosteric Site within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:11.2 occ:1.00 CL A:TOW401 0.0 11.2 1.0 C8 A:TOW401 1.7 9.9 1.0 C9 A:TOW401 2.7 10.5 1.0 C7 A:TOW401 2.7 10.3 1.0 C10 A:TOW401 4.0 11.1 1.0 C6 A:TOW401 4.0 9.2 1.0 C11 A:TOW401 4.5 9.9 1.0 CE2 A:PHE20 4.6 10.9 1.0 O1 A:TOW401 4.9 9.1 0.4 CD2 A:PHE20 4.9 10.6 1.0

C.De Fusco, M.Schimpl, C.De Fusco, U.Borjesson, T.Cheung, I.Collie, L.Evans, P.Narasimhan, C.Stubbs, M.Vazquez-Chantada, D.J.Wagner, M.Grondine, S.Tentarelli, E.Underwood, A.Argyrou, S.Bagal, E.Chiarparin, G.Robb, J.S.Scott. N/A N/A.
ISSN: ISSN 0022-2623
DOI: 10.1021/ACS.JMEDCHEM.1C00067