Mercury in PDB 6hp1: Crystal Structure of the O-Methyltransferase From the Trans-at Pks Multienzyme C0ZGQ3 of Brevibacillus Brevis

The structure of Crystal Structure of the O-Methyltransferase From the Trans-at Pks Multienzyme C0ZGQ3 of Brevibacillus Brevis, PDB code: 6hp1 was solved by R.P.Jakob, P.Felber, Y.Demyanenko, F.Delbart, T.Maier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.74 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	44.613, 71.760, 61.192, 90.00, 104.07, 90.00
R / Rfree (%)	17.3 / 20.5

The binding sites of Mercury atom in the Crystal Structure of the O-Methyltransferase From the Trans-at Pks Multienzyme C0ZGQ3 of Brevibacillus Brevis (pdb code 6hp1). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 4 binding sites of Mercury where determined in the Crystal Structure of the O-Methyltransferase From the Trans-at Pks Multienzyme C0ZGQ3 of Brevibacillus Brevis, PDB code: 6hp1:
Jump to Mercury binding site number: 1; 2; 3; 4;

Mercury binding site 1 out of 4 in the Crystal Structure of the O-Methyltransferase From the Trans-at Pks Multienzyme C0ZGQ3 of Brevibacillus Brevis


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 the O-Methyltransferase From the Trans-at Pks Multienzyme C0ZGQ3 of Brevibacillus Brevis within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg401 b:48.9 occ:0.24 HG A:EMC401 0.0 48.9 0.2 C1 A:EMC401 2.0 32.1 0.2 H12 A:EMC401 2.6 38.5 0.2 H11 A:EMC401 2.6 38.5 0.2 HE3 A:MET1181 2.7 42.0 1.0 HA A:VAL1169 2.7 42.8 1.0 H22 A:EMC401 2.8 30.2 0.2 H A:CYS1170 2.9 34.0 1.0 C2 A:EMC401 2.9 25.1 0.2 HE1 A:MET1181 3.0 42.0 1.0 HG13 A:VAL1198 3.0 29.6 1.0 HG11 A:VAL1198 3.0 29.6 1.0 SG A:CYS1170 3.0 31.2 1.0 N A:CYS1170 3.1 28.3 1.0 HB3 A:CYS1170 3.1 31.1 1.0 CE A:MET1181 3.1 35.0 1.0 H21 A:EMC401 3.2 30.2 0.2 C A:VAL1169 3.4 34.3 1.0 CG1 A:VAL1198 3.4 24.6 1.0 CB A:CYS1170 3.5 25.9 1.0 CA A:VAL1169 3.5 35.7 1.0 SD A:MET1181 3.6 33.0 1.0 O A:THR1168 3.7 34.2 1.0 H23 A:EMC401 3.7 30.2 0.2 HG12 A:VAL1198 3.8 29.6 1.0 CA A:CYS1170 3.8 24.0 1.0 HD11 A:ILE1185 3.9 45.3 1.0 HE2 A:MET1181 4.1 42.0 1.0 HG2 A:MET1181 4.1 36.3 1.0 HE21 A:GLN1202 4.1 39.9 1.0 HB A:VAL1169 4.2 37.1 1.0 O A:VAL1169 4.3 35.9 1.0 HG3 A:GLN1202 4.3 31.6 1.0 HG2 A:GLN1202 4.3 31.6 1.0 HB2 A:CYS1170 4.4 31.1 1.0 CB A:VAL1169 4.4 30.9 1.0 CG A:MET1181 4.5 30.2 1.0 N A:VAL1169 4.5 40.2 1.0 C A:THR1168 4.5 40.1 1.0 HB1 A:ALA1370 4.5 27.8 1.0 NE2 A:GLN1202 4.6 33.2 1.0 HA A:CYS1170 4.6 28.8 1.0 HG12 A:VAL1169 4.6 40.2 1.0 O A:CYS1170 4.6 23.3 1.0 HG13 A:ILE1185 4.7 39.5 1.0 HG22 A:VAL1198 4.7 25.8 1.0 HD21 A:LEU1371 4.7 41.9 1.0 HD23 A:LEU1371 4.7 41.9 1.0 C A:CYS1170 4.7 22.4 1.0 CG A:GLN1202 4.7 26.3 1.0 CB A:VAL1198 4.8 23.2 1.0 CD1 A:ILE1185 4.8 37.8 1.0 HG21 A:VAL1198 4.8 25.8 1.0 HG3 A:MET1181 4.8 36.3 1.0 CD A:GLN1202 4.9 29.1 1.0 HE22 A:GLN1202 5.0 39.9 1.0

Mercury binding site 2 out of 4 in the Crystal Structure of the O-Methyltransferase From the Trans-at Pks Multienzyme C0ZGQ3 of Brevibacillus Brevis


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 the O-Methyltransferase From the Trans-at Pks Multienzyme C0ZGQ3 of Brevibacillus Brevis within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg402 b:35.4 occ:0.20 HG A:EMC402 0.0 35.4 0.2 C1 A:EMC402 2.0 18.6 0.2 SG A:CYS1211 2.5 21.7 1.0 H12 A:EMC402 2.5 22.3 0.2 H11 A:EMC402 2.5 22.3 0.2 O A:HOH592 2.6 24.8 1.0 HG2 A:LYS1212 2.8 37.1 1.0 H22 A:EMC402 2.8 15.2 0.2 HE2 A:LYS1212 2.9 57.4 1.0 HE3 A:LYS1212 3.0 57.4 1.0 C2 A:EMC402 3.0 12.7 0.2 O A:HOH536 3.0 24.0 1.0 H21 A:EMC402 3.3 15.2 0.2 CE A:LYS1212 3.4 47.8 1.0 HB2 A:CYS1211 3.4 22.2 1.0 HA A:MET1445 3.5 23.3 1.0 O A:CYS1211 3.5 24.6 1.0 CB A:CYS1211 3.6 18.5 1.0 CG A:LYS1212 3.7 30.9 1.0 H23 A:EMC402 3.7 15.2 0.2 HB2 A:MET1445 3.8 26.1 1.0 C A:CYS1211 3.8 21.6 1.0 HG3 A:MET1445 3.9 29.6 1.0 HG3 A:LYS1212 4.0 37.1 1.0 O A:HOH530 4.1 25.9 1.0 CD A:LYS1212 4.1 43.1 1.0 HA A:LYS1212 4.2 24.4 1.0 CA A:MET1445 4.2 19.4 1.0 N A:LYS1212 4.3 19.3 1.0 OE2 A:GLU1444 4.3 35.8 1.0 HD3 A:LYS1212 4.3 51.8 1.0 CA A:CYS1211 4.3 19.8 1.0 HG2 A:GLU1444 4.3 34.1 1.0 CB A:MET1445 4.3 21.8 1.0 HB3 A:CYS1211 4.3 22.2 1.0 CG A:MET1445 4.6 24.7 1.0 NZ A:LYS1212 4.6 51.8 1.0 CA A:LYS1212 4.6 20.3 1.0 HZ2 A:LYS1212 4.7 62.1 1.0 N A:MET1445 4.7 19.6 1.0 H A:LYS1212 4.7 23.2 1.0 OG A:SER1448 4.8 27.8 1.0 CB A:LYS1212 4.8 23.4 1.0 HZ1 A:LYS1412 4.8 25.1 1.0 H A:MET1445 4.8 23.6 1.0 HD2 A:TYR1450 4.8 26.4 1.0 HD2 A:LYS1212 4.9 51.8 1.0 HB3 A:SER1448 4.9 35.2 1.0 HG A:SER1448 5.0 33.4 1.0

Mercury binding site 3 out of 4 in the Crystal Structure of the O-Methyltransferase From the Trans-at Pks Multienzyme C0ZGQ3 of Brevibacillus Brevis


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 the O-Methyltransferase From the Trans-at Pks Multienzyme C0ZGQ3 of Brevibacillus Brevis within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg403 b:54.2 occ:0.27 HG A:EMC403 0.0 54.2 0.3 C1 A:EMC403 2.0 38.3 0.3 HB3 A:CYS1425 2.2 39.4 1.0 H11 A:EMC403 2.6 46.0 0.3 H12 A:EMC403 2.6 46.0 0.3 C2 A:EMC403 2.9 36.7 0.3 H23 A:EMC403 2.9 44.0 0.3 H22 A:EMC403 3.0 44.0 0.3 CB A:CYS1425 3.1 32.9 1.0 C A:CYS1425 3.3 28.4 1.0 O A:CYS1425 3.3 32.0 1.0 HA A:GLU1426 3.5 41.5 1.0 HG21 A:ILE1347 3.5 30.6 1.0 HB2 A:ALA1429 3.7 36.7 1.0 N A:GLU1426 3.7 30.2 1.0 HB2 A:CYS1425 3.7 39.4 1.0 H21 A:EMC403 3.7 44.0 0.3 CA A:CYS1425 3.8 29.1 1.0 HE22 A:GLN1344 3.8 81.8 1.0 HG3 A:GLU1426 3.8 61.7 1.0 SG A:CYS1425 3.9 36.5 1.0 HG A:CYS1425 4.0 43.9 1.0 HG22 A:ILE1347 4.1 30.6 1.0 H A:GLU1426 4.1 36.3 1.0 CA A:GLU1426 4.1 34.5 1.0 HA A:CYS1425 4.1 35.0 1.0 CG2 A:ILE1347 4.2 25.5 1.0 HG2 A:GLU1426 4.3 61.7 1.0 HB3 A:ALA1429 4.4 36.7 1.0 CB A:ALA1429 4.4 30.6 1.0 CG A:GLU1426 4.5 51.4 1.0 HG23 A:ILE1347 4.5 30.6 1.0 NE2 A:GLN1344 4.6 68.2 1.0 HD13 A:ILE1347 4.7 49.8 1.0 HB1 A:ALA1429 4.8 36.7 1.0 H A:ALA1429 4.9 32.5 1.0 CB A:GLU1426 4.9 41.9 1.0 HE21 A:GLN1344 4.9 81.8 1.0 O A:THR1422 5.0 35.0 1.0

Mercury binding site 4 out of 4 in the Crystal Structure of the O-Methyltransferase From the Trans-at Pks Multienzyme C0ZGQ3 of Brevibacillus Brevis


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 4 of Crystal Structure of the O-Methyltransferase From the Trans-at Pks Multienzyme C0ZGQ3 of Brevibacillus Brevis within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg404 b:32.1 occ:0.17 HG A:EMC404 0.0 32.1 0.2 N A:GLY1229 1.3 43.5 0.6 H A:GLY1229 1.4 52.2 0.6 C A:HIS1228 1.8 47.5 0.6 C1 A:EMC404 2.3 19.3 0.2 O A:GLY1227 2.3 47.9 0.6 CA A:GLY1229 2.4 30.4 0.6 O A:HIS1228 2.5 45.9 0.6 HA3 A:GLY1229 2.6 36.6 0.6 CA A:HIS1228 2.6 45.9 0.6 C A:GLY1227 2.6 46.0 0.6 HA2 A:GLY1229 2.6 36.6 0.6 HD13 A:ILE1272 2.7 43.2 1.0 H12 A:EMC404 2.8 23.2 0.2 H11 A:EMC404 2.8 23.2 0.2 HA A:HIS1228 2.8 55.1 0.6 O A:CYS1226 2.8 36.8 1.0 N A:HIS1228 2.8 47.2 0.6 HA2 A:GLY1227 3.0 53.0 0.4 SG A:CYS1226 3.0 29.2 1.0 H21 A:EMC404 3.1 25.2 0.2 C2 A:EMC404 3.1 21.0 0.2 H22 A:EMC404 3.2 25.2 0.2 C A:CYS1226 3.2 36.9 1.0 HB2 A:CYS1226 3.4 35.2 1.0 HG21 A:ILE1272 3.5 35.4 1.0 H A:HIS1228 3.5 56.7 0.6 CD1 A:ILE1272 3.6 36.0 1.0 N A:GLY1227 3.6 39.8 0.4 N A:GLY1227 3.6 39.8 0.6 CA A:GLY1227 3.7 44.1 0.4 CB A:CYS1226 3.7 29.3 1.0 CA A:GLY1227 3.7 44.1 0.6 HD11 A:ILE1272 3.8 43.2 1.0 C A:GLY1229 3.8 31.6 0.6 H23 A:EMC404 4.0 25.2 0.2 O A:GLY1227 4.0 52.9 0.4 CA A:CYS1226 4.1 32.3 1.0 HA3 A:GLY1227 4.1 53.0 0.6 HA3 A:GLY1257 4.1 39.1 1.0 CB A:HIS1228 4.1 47.6 0.6 HD12 A:ILE1272 4.1 43.2 1.0 HG12 A:ILE1272 4.2 42.2 1.0 HB A:THR1248 4.2 36.3 1.0 C A:GLY1227 4.2 49.9 0.4 HB3 A:GLN1253 4.2 51.3 1.0 HG21 A:THR1248 4.2 37.2 1.0 O A:GLY1229 4.2 47.9 0.4 H A:THR1230 4.2 54.7 0.6 H A:GLY1227 4.3 47.8 0.4 H A:GLY1227 4.3 47.8 0.6 CG2 A:ILE1272 4.3 29.5 1.0 HG23 A:ILE1272 4.3 35.4 1.0 HB2 A:HIS1228 4.4 57.1 0.6 CG1 A:ILE1272 4.4 35.1 1.0 N A:THR1230 4.4 45.6 0.6 HA2 A:GLY1227 4.4 53.0 0.6 O A:GLN1253 4.5 30.8 1.0 HA3 A:GLY1227 4.5 53.0 0.4 HG21 A:VAL1232 4.5 80.1 1.0 HG22 A:VAL1232 4.5 80.1 1.0 HB3 A:CYS1226 4.6 35.2 1.0 HB3 A:HIS1228 4.7 57.1 0.6 O A:GLY1229 4.7 30.1 0.6 HA A:CYS1226 4.7 38.8 1.0 HA A:ALA1254 4.8 39.5 1.0 CG2 A:THR1248 4.9 30.9 1.0 HG22 A:THR1248 4.9 37.2 1.0 CG A:HIS1228 4.9 51.0 0.6 CB A:THR1248 4.9 30.2 1.0 CA A:GLY1257 5.0 32.6 1.0 CG2 A:VAL1232 5.0 66.7 1.0

R.P.Jakob, P.Felber, Y.Demyanenko, F.Delbart, T.Maier. Structural and Functional Analysis of An O-Methyltransferase From the Trans-at Pks Biosynthesis Pathway To Be Published.