Chlorine in PDB 7kdb: Crystal Structure of Human Methionine Adenosyltransferase 2A (MAT2A) in Complex with Sam and Allosteric Inhibitor Compound 35

All present enzymatic activity of Crystal Structure of Human Methionine Adenosyltransferase 2A (MAT2A) in Complex with Sam and Allosteric Inhibitor Compound 35:
2.5.1.6;

The structure of Crystal Structure of Human Methionine Adenosyltransferase 2A (MAT2A) in Complex with Sam and Allosteric Inhibitor Compound 35, PDB code: 7kdb was solved by A.Padyana, L.Jin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.88 / 1.24
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	68.11, 94.027, 116.795, 90, 90, 90
R / Rfree (%)	12.6 / 13.8

The binding sites of Chlorine atom in the Crystal Structure of Human Methionine Adenosyltransferase 2A (MAT2A) in Complex with Sam and Allosteric Inhibitor Compound 35 (pdb code 7kdb). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Human Methionine Adenosyltransferase 2A (MAT2A) in Complex with Sam and Allosteric Inhibitor Compound 35, PDB code: 7kdb:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Human Methionine Adenosyltransferase 2A (MAT2A) in Complex with Sam and Allosteric Inhibitor Compound 35


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 Human Methionine Adenosyltransferase 2A (MAT2A) in Complex with Sam and Allosteric Inhibitor Compound 35 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:9.8 occ:1.00 HE2 A:HIS29 2.3 7.9 1.0 HZ2 A:LYS181 2.4 9.3 1.0 HZ3 A:LYS265 2.4 12.2 1.0 H4' A:SAM409 3.1 8.3 1.0 NE2 A:HIS29 3.1 6.6 1.0 HZ1 A:LYS181 3.1 9.3 1.0 H5'1 A:SAM409 3.1 9.8 1.0 NZ A:LYS181 3.1 7.8 1.0 NZ A:LYS265 3.3 10.2 1.0 O A:HOH527 3.3 32.6 1.0 O A:HOH864 3.3 29.0 1.0 HE1 A:HIS29 3.4 7.3 1.0 H5'2 A:SAM409 3.4 9.8 1.0 HE3 A:LYS265 3.5 11.8 1.0 HE2 A:LYS265 3.5 11.8 1.0 C5' A:SAM409 3.6 8.2 1.0 CE1 A:HIS29 3.6 6.1 1.0 O A:HOH925 3.6 35.5 1.0 HE3 A:LYS181 3.7 8.5 1.0 CE A:LYS265 3.7 9.8 1.0 HZ2 A:LYS265 3.7 12.2 1.0 HZ1 A:LYS265 3.8 12.2 1.0 HZ3 A:LYS181 3.8 9.3 1.0 C4' A:SAM409 3.8 6.9 1.0 HD2 A:LYS181 3.9 8.8 1.0 CE A:LYS181 3.9 7.1 1.0 O A:HOH625 4.1 19.1 1.0 OD2 A:ASP31 4.2 7.9 1.0 OD2 A:ASP258 4.2 12.2 1.0 O3' A:SAM409 4.2 7.3 1.0 HO3' A:SAM409 4.2 8.8 1.0 CD2 A:HIS29 4.3 5.9 1.0 CD A:LYS181 4.5 7.3 1.0 O A:HOH599 4.5 8.9 1.0 HD2 A:HIS29 4.6 7.0 1.0 C3' A:SAM409 4.7 5.8 1.0 O A:HOH629 4.7 40.1 1.0 HE2 A:LYS181 4.8 8.5 1.0 HG11 A:VAL25 4.8 7.2 1.0 HG1 A:SAM409 4.9 20.4 1.0 ND1 A:HIS29 4.9 6.6 1.0 HG2 A:SAM409 4.9 20.4 1.0 O4' A:SAM409 4.9 6.5 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Human Methionine Adenosyltransferase 2A (MAT2A) in Complex with Sam and Allosteric Inhibitor Compound 35


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Human Methionine Adenosyltransferase 2A (MAT2A) in Complex with Sam and Allosteric Inhibitor Compound 35 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl407 b:66.4 occ:1.00 HH22 A:ARG177 1.7 18.7 0.5 NH2 A:ARG177 2.3 15.6 0.5 HG3 A:GLU211 2.4 24.4 0.4 H A:GLU211 2.5 15.2 0.6 H A:GLU211 2.5 15.2 0.4 O A:HOH507 2.7 29.7 1.0 HH21 A:ARG177 2.7 18.7 0.5 HH21 A:ARG177 3.0 10.1 0.3 O A:HOH693 3.0 43.1 1.0 HA A:ASP210 3.1 10.5 1.0 HB2 A:GLU211 3.1 20.8 0.6 HH12 A:ARG177 3.1 9.6 0.5 CZ A:ARG177 3.2 13.6 0.5 N A:GLU211 3.3 12.7 1.0 HB2 A:GLU211 3.3 20.9 0.4 CG A:GLU211 3.3 20.4 0.4 HB2 A:ASP210 3.3 13.9 1.0 NH1 A:ARG177 3.5 8.0 0.5 HB3 A:GLU211 3.5 20.8 0.6 CB A:GLU211 3.7 17.4 0.6 HG13 A:VAL251 3.7 10.1 1.0 CB A:GLU211 3.7 17.4 0.4 NH2 A:ARG177 3.7 8.4 0.3 CA A:ASP210 3.8 8.8 1.0 O A:SER96 3.9 15.9 1.0 CD A:GLU211 4.0 21.9 0.4 HE A:ARG177 4.0 9.0 0.3 C A:ASP210 4.0 9.2 1.0 HG2 A:GLU211 4.0 24.4 0.4 CB A:ASP210 4.0 11.6 1.0 CA A:GLU211 4.1 16.7 0.6 HH22 A:ARG177 4.1 10.1 0.3 CA A:GLU211 4.1 13.8 0.4 HB2 A:SER96 4.1 18.4 1.0 OE2 A:GLU211 4.3 25.1 0.4 HH11 A:ARG177 4.3 9.6 0.5 HG11 A:VAL251 4.3 10.1 1.0 NE A:ARG177 4.4 15.6 0.5 CG1 A:VAL251 4.4 8.4 1.0 HB3 A:ASP210 4.5 13.9 1.0 HH21 A:ARG177 4.5 25.6 0.3 HA A:GLU211 4.5 20.1 0.6 HE A:ARG177 4.6 18.7 0.5 HA A:GLU211 4.6 16.5 0.4 CZ A:ARG177 4.6 7.9 0.3 HG12 A:VAL251 4.6 10.1 1.0 NE A:ARG177 4.6 7.5 0.3 OE1 A:GLU211 4.6 28.4 0.4 HB3 A:GLU211 4.6 20.9 0.4 HE A:ARG177 4.7 9.1 0.3 OE2 A:GLU212 4.7 50.0 1.0 O A:HOH509 4.9 34.5 1.0 C A:SER96 4.9 11.8 1.0 O A:HIS209 4.9 7.9 1.0

Z.Konteatis, J.Travins, S.Gross, K.Marjon, A.Barnett, E.Mandley, B.Nicolay, R.Nagaraja, Y.Chen, Y.Sun, Z.Liu, J.Yu, Z.Ye, F.Jiang, W.Wei, C.Fang, Y.Gao, P.Kalev, M.L.Hyer, B.Delabarre, L.Jin, A.K.Padyana, L.Dang, J.Murtie, S.A.Biller, Z.Sui, K.M.Marks. Discovery of Ag-270, A First-in-Class Oral MAT2A Inhibitor For the Treatment of Tumors with Homozygous Mtap Deletion. J.Med.Chem. 2021.
ISSN: ISSN 0022-2623
PubMed: 33829783
DOI: 10.1021/ACS.JMEDCHEM.0C01895