Mercury in PDB 2v7e: Crystal Structure of Coactivator-Associated Arginine Methyltransferase 1 (CARM1), Unliganded

The structure of Crystal Structure of Coactivator-Associated Arginine Methyltransferase 1 (CARM1), Unliganded, PDB code: 2v7e was solved by W.W.Yue, M.Hassler, S.M.Roe, V.Thompson-Vale, L.H.Pearl, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.69 / 2.70
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	74.146, 98.018, 206.915, 90.00, 90.00, 90.00
R / Rfree (%)	22.8 / 27.6

The binding sites of Mercury atom in the Crystal Structure of Coactivator-Associated Arginine Methyltransferase 1 (CARM1), Unliganded (pdb code 2v7e). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 3 binding sites of Mercury where determined in the Crystal Structure of Coactivator-Associated Arginine Methyltransferase 1 (CARM1), Unliganded, PDB code: 2v7e:
Jump to Mercury binding site number: 1; 2; 3;

Mercury binding site 1 out of 3 in the Crystal Structure of Coactivator-Associated Arginine Methyltransferase 1 (CARM1), Unliganded


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Crystal Structure of Coactivator-Associated Arginine Methyltransferase 1 (CARM1), Unliganded within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg1477 b:0.5 occ:0.50 CD1 A:ILE453 2.6 41.0 1.0 CB A:CYS421 3.5 40.3 1.0 CD2 A:LEU468 3.5 42.3 1.0 CG1 A:ILE453 4.0 40.8 1.0 N A:CYS421 4.1 40.4 1.0 O A:LEU388 4.3 40.8 1.0 SG A:CYS439 4.3 39.5 1.0 CE A:MET263 4.4 42.4 1.0 CA A:CYS421 4.4 40.2 1.0 CB A:LEU388 4.5 40.7 1.0 SD A:MET263 4.7 42.4 1.0 SG A:CYS421 4.9 40.9 1.0 CB A:PHE390 4.9 41.7 1.0 CD1 A:LEU388 5.0 40.0 1.0 C A:LEU388 5.0 40.9 1.0

Mercury binding site 2 out of 3 in the Crystal Structure of Coactivator-Associated Arginine Methyltransferase 1 (CARM1), Unliganded


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Crystal Structure of Coactivator-Associated Arginine Methyltransferase 1 (CARM1), Unliganded within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg1478 b:0.6 occ:0.50 SG A:CYS421 1.4 40.9 1.0 O A:LEU422 3.1 39.2 1.0 CB A:CYS421 3.2 40.3 1.0 CB A:ASN466 3.2 42.6 1.0 CG A:ASN466 3.5 43.0 1.0 C A:LEU422 3.5 39.3 1.0 ND2 A:ASN466 3.8 43.3 1.0 CD1 A:PHE423 3.8 37.9 1.0 C A:CYS421 3.9 40.0 1.0 N A:PHE423 3.9 38.8 1.0 N A:LEU422 3.9 39.7 1.0 CA A:CYS421 4.0 40.2 1.0 CA A:PHE423 4.0 38.3 1.0 OD1 A:ASN466 4.0 43.3 1.0 CA A:LEU422 4.3 39.5 1.0 O A:CYS421 4.3 40.0 1.0 CE1 A:PHE423 4.4 37.5 1.0 O A:PHE336 4.5 41.4 1.0 CA A:ASN466 4.7 42.6 1.0 CG A:PHE423 4.7 38.1 1.0 CB A:ILE453 4.7 40.6 1.0 CD1 A:ILE453 4.8 41.0 1.0 CB A:PHE423 4.9 38.5 1.0 CG1 A:ILE453 5.0 40.8 1.0

Mercury binding site 3 out of 3 in the Crystal Structure of Coactivator-Associated Arginine Methyltransferase 1 (CARM1), Unliganded


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of Crystal Structure of Coactivator-Associated Arginine Methyltransferase 1 (CARM1), Unliganded within 5.0Å range: probe atom residue distance (Å) B Occ B:Hg1477 b:83.0 occ:0.50 OD2 B:ASP191 2.4 42.7 1.0 SG B:CYS194 2.7 30.6 1.0 CG B:ASP191 3.4 41.5 1.0 CA B:CYS194 3.4 37.2 1.0 CB B:CYS194 3.6 37.2 1.0 N B:CYS194 3.8 38.2 1.0 OD1 B:ASP191 3.8 42.4 1.0 O B:GLY193 4.1 38.9 1.0 C B:GLY193 4.1 38.7 1.0 CA B:GLY197 4.5 37.0 1.0 CB B:ASP191 4.5 40.5 1.0 O B:ASP191 4.6 40.3 1.0 C B:CYS194 4.8 37.7 1.0 O B:HOH2007 4.8 17.6 1.0 C B:GLY197 4.9 36.9 1.0 O B:GLY197 4.9 36.8 1.0 N B:GLY195 5.0 37.7 1.0 CB B:ALA213 5.0 40.7 1.0

W.W.Yue, M.Hassler, S.M.Roe, V.Thompson-Vale, L.H.Pearl. Insights Into Histone Code Syntax From Structural and Biochemical Studies of CARM1 Methyltransferase Embo J. V. 26 4402 2007.
ISSN: ISSN 0261-4189
PubMed: 17882261
DOI: 10.1038/SJ.EMBOJ.7601856