Mercury in PDB 6hp1: Crystal Structure of the O-Methyltransferase From the Trans-at Pks Multienzyme C0ZGQ3 of Brevibacillus Brevis
Protein crystallography data
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
|
Mercury Binding Sites:
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 6hp1
Go back to
Mercury Binding Sites List in 6hp1
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 6hp1
Go back to
Mercury Binding Sites List in 6hp1
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 6hp1
Go back to
Mercury Binding Sites List in 6hp1
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 6hp1
Go back to
Mercury Binding Sites List in 6hp1
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
|
|
Reference:
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.
Page generated: Sun Aug 11 07:19:59 2024
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