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

Protein crystallography data

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

Mercury Binding Sites:

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 2v7e

Go back to Mercury Binding Sites List in 2v7e
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 2v7e

Go back to Mercury Binding Sites List in 2v7e
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 2v7e

Go back to Mercury Binding Sites List in 2v7e
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

Reference:

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
Page generated: Sun Dec 13 19:08:24 2020

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