Chlorine in PDB 7bhw: Crystal Structure of MAT2A Bound to Allosteric Inhibitor (Compound 29)

All present enzymatic activity of Crystal Structure of MAT2A Bound to Allosteric Inhibitor (Compound 29):
2.5.1.6;

The structure of Crystal Structure of MAT2A Bound to Allosteric Inhibitor (Compound 29), PDB code: 7bhw 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 (°)	68.58, 94.199, 117.404, 90, 90, 90
R / Rfree (%)	15.5 / 16.7

The binding sites of Chlorine atom in the Crystal Structure of MAT2A Bound to Allosteric Inhibitor (Compound 29) (pdb code 7bhw). 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 Bound to Allosteric Inhibitor (Compound 29), PDB code: 7bhw:

Chlorine binding site 1 out of 1 in the Crystal Structure of MAT2A Bound to Allosteric Inhibitor (Compound 29)


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 Bound to Allosteric Inhibitor (Compound 29) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:12.3 occ:1.00 CL A:TNW401 0.0 12.3 1.0 C13 A:TNW401 1.7 12.1 1.0 C12 A:TNW401 2.7 11.1 1.0 C14 A:TNW401 2.7 12.1 1.0 C15 A:TNW401 4.0 12.1 1.0 C11 A:TNW401 4.0 10.7 1.0 C16 A:TNW401 4.5 11.0 1.0 CE2 A:PHE20 4.7 11.8 1.0 CD2 A:PHE20 4.9 10.9 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