Cobalt in PDB 2i2x: Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri
Enzymatic activity of Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri
All present enzymatic activity of Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri:
2.1.1.90;
Protein crystallography data
The structure of Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri, PDB code: 2i2x
was solved by
C.H.Hagemeier,
M.Kruer,
R.K.Thauer,
E.Warkentin,
U.Ermler,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
20.00 /
2.50
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
101.750,
172.850,
190.540,
90.00,
98.86,
90.00
|
R / Rfree (%)
|
18.2 /
23.1
|
Other elements in 2i2x:
The structure of Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri also contains other interesting chemical elements:
Cobalt Binding Sites:
The binding sites of Cobalt atom in the Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri
(pdb code 2i2x). This binding sites where shown within
5.0 Angstroms radius around Cobalt atom.
In total 8 binding sites of Cobalt where determined in the
Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri, PDB code: 2i2x:
Jump to Cobalt binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Cobalt binding site 1 out
of 8 in 2i2x
Go back to
Cobalt Binding Sites List in 2i2x
Cobalt binding site 1 out
of 8 in the Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 1 of Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Co500
b:19.2
occ:1.00
|
CO
|
B:B13500
|
0.0
|
19.2
|
1.0
|
N24
|
B:B13500
|
1.8
|
17.7
|
1.0
|
N21
|
B:B13500
|
1.8
|
20.0
|
1.0
|
N22
|
B:B13500
|
1.9
|
20.5
|
1.0
|
N23
|
B:B13500
|
1.9
|
17.4
|
1.0
|
NE2
|
B:HIS136
|
2.5
|
39.9
|
1.0
|
C19
|
B:B13500
|
2.8
|
18.9
|
1.0
|
C1
|
B:B13500
|
2.8
|
20.1
|
1.0
|
C9
|
B:B13500
|
2.8
|
22.1
|
1.0
|
C11
|
B:B13500
|
2.9
|
16.2
|
1.0
|
C4
|
B:B13500
|
2.9
|
19.8
|
1.0
|
C16
|
B:B13500
|
2.9
|
18.4
|
1.0
|
C14
|
B:B13500
|
3.0
|
16.1
|
1.0
|
C6
|
B:B13500
|
3.0
|
23.2
|
1.0
|
C10
|
B:B13500
|
3.2
|
19.8
|
1.0
|
O
|
B:HOH501
|
3.2
|
42.7
|
1.0
|
C20
|
B:B13500
|
3.3
|
16.1
|
1.0
|
C5
|
B:B13500
|
3.4
|
22.9
|
1.0
|
C15
|
B:B13500
|
3.4
|
15.0
|
1.0
|
CD2
|
B:HIS136
|
3.4
|
40.1
|
1.0
|
CE1
|
B:HIS136
|
3.5
|
40.1
|
1.0
|
C18
|
B:B13500
|
4.1
|
20.1
|
1.0
|
C2
|
B:B13500
|
4.1
|
20.9
|
1.0
|
C8
|
B:B13500
|
4.2
|
24.1
|
1.0
|
C3
|
B:B13500
|
4.2
|
20.7
|
1.0
|
C17
|
B:B13500
|
4.2
|
20.6
|
1.0
|
C13
|
B:B13500
|
4.3
|
16.2
|
1.0
|
C12
|
B:B13500
|
4.3
|
16.5
|
1.0
|
C7
|
B:B13500
|
4.3
|
25.2
|
1.0
|
C26
|
B:B13500
|
4.6
|
22.4
|
1.0
|
ND1
|
B:HIS136
|
4.6
|
41.7
|
1.0
|
CG
|
B:HIS136
|
4.6
|
41.8
|
1.0
|
C37
|
B:B13500
|
4.8
|
28.1
|
1.0
|
C41
|
B:B13500
|
4.8
|
27.1
|
1.0
|
C53
|
B:B13500
|
4.9
|
16.5
|
1.0
|
C35
|
B:B13500
|
4.9
|
21.9
|
1.0
|
C54
|
B:B13500
|
5.0
|
19.6
|
1.0
|
|
Cobalt binding site 2 out
of 8 in 2i2x
Go back to
Cobalt Binding Sites List in 2i2x
Cobalt binding site 2 out
of 8 in the Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 2 of Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Co500
b:27.6
occ:1.00
|
CO
|
D:B13500
|
0.0
|
27.6
|
1.0
|
N24
|
D:B13500
|
1.8
|
26.9
|
1.0
|
N21
|
D:B13500
|
1.8
|
28.1
|
1.0
|
N22
|
D:B13500
|
1.9
|
31.7
|
1.0
|
N23
|
D:B13500
|
1.9
|
29.5
|
1.0
|
NE2
|
D:HIS136
|
2.4
|
43.2
|
1.0
|
C19
|
D:B13500
|
2.7
|
26.7
|
1.0
|
C9
|
D:B13500
|
2.8
|
32.9
|
1.0
|
C1
|
D:B13500
|
2.8
|
26.4
|
1.0
|
C11
|
D:B13500
|
2.9
|
29.2
|
1.0
|
C4
|
D:B13500
|
2.9
|
28.3
|
1.0
|
C16
|
D:B13500
|
2.9
|
26.0
|
1.0
|
C6
|
D:B13500
|
3.0
|
33.3
|
1.0
|
C14
|
D:B13500
|
3.0
|
27.3
|
1.0
|
C10
|
D:B13500
|
3.2
|
30.7
|
1.0
|
O
|
D:HOH501
|
3.3
|
20.5
|
1.0
|
CE1
|
D:HIS136
|
3.3
|
43.6
|
1.0
|
CD2
|
D:HIS136
|
3.4
|
44.9
|
1.0
|
C5
|
D:B13500
|
3.4
|
31.3
|
1.0
|
C15
|
D:B13500
|
3.5
|
25.7
|
1.0
|
C20
|
D:B13500
|
3.5
|
22.9
|
1.0
|
C18
|
D:B13500
|
4.1
|
27.8
|
1.0
|
C2
|
D:B13500
|
4.1
|
27.8
|
1.0
|
C8
|
D:B13500
|
4.2
|
34.6
|
1.0
|
C3
|
D:B13500
|
4.2
|
27.3
|
1.0
|
C17
|
D:B13500
|
4.2
|
25.2
|
1.0
|
C12
|
D:B13500
|
4.3
|
29.4
|
1.0
|
C13
|
D:B13500
|
4.3
|
28.4
|
1.0
|
C7
|
D:B13500
|
4.3
|
34.8
|
1.0
|
C26
|
D:B13500
|
4.4
|
25.9
|
1.0
|
ND1
|
D:HIS136
|
4.4
|
45.2
|
1.0
|
CG
|
D:HIS136
|
4.5
|
46.0
|
1.0
|
C37
|
D:B13500
|
4.9
|
36.2
|
1.0
|
C46
|
D:B13500
|
4.9
|
27.5
|
1.0
|
C41
|
D:B13500
|
4.9
|
37.2
|
1.0
|
C54
|
D:B13500
|
4.9
|
23.8
|
1.0
|
C35
|
D:B13500
|
4.9
|
29.3
|
1.0
|
|
Cobalt binding site 3 out
of 8 in 2i2x
Go back to
Cobalt Binding Sites List in 2i2x
Cobalt binding site 3 out
of 8 in the Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 3 of Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Co500
b:65.9
occ:1.00
|
CO
|
F:B13500
|
0.0
|
65.9
|
1.0
|
N24
|
F:B13500
|
1.8
|
64.9
|
1.0
|
N21
|
F:B13500
|
1.8
|
64.7
|
1.0
|
N22
|
F:B13500
|
1.9
|
66.5
|
1.0
|
N23
|
F:B13500
|
1.9
|
65.5
|
1.0
|
NE2
|
F:HIS136
|
2.7
|
57.9
|
1.0
|
C19
|
F:B13500
|
2.8
|
64.2
|
1.0
|
C1
|
F:B13500
|
2.8
|
64.2
|
1.0
|
C9
|
F:B13500
|
2.9
|
66.7
|
1.0
|
C4
|
F:B13500
|
2.9
|
64.7
|
1.0
|
C11
|
F:B13500
|
2.9
|
65.8
|
1.0
|
C16
|
F:B13500
|
2.9
|
64.5
|
1.0
|
C14
|
F:B13500
|
3.0
|
65.5
|
1.0
|
C6
|
F:B13500
|
3.0
|
67.6
|
1.0
|
C10
|
F:B13500
|
3.2
|
65.7
|
1.0
|
O
|
F:HOH501
|
3.2
|
17.7
|
0.5
|
C5
|
F:B13500
|
3.4
|
66.3
|
1.0
|
C15
|
F:B13500
|
3.4
|
64.7
|
1.0
|
C20
|
F:B13500
|
3.4
|
63.8
|
1.0
|
CE1
|
F:HIS136
|
3.5
|
57.2
|
1.0
|
CD2
|
F:HIS136
|
3.7
|
58.1
|
1.0
|
C18
|
F:B13500
|
4.1
|
63.5
|
1.0
|
C2
|
F:B13500
|
4.1
|
63.9
|
1.0
|
C3
|
F:B13500
|
4.2
|
63.8
|
1.0
|
C17
|
F:B13500
|
4.2
|
63.5
|
1.0
|
C8
|
F:B13500
|
4.2
|
68.0
|
1.0
|
C12
|
F:B13500
|
4.3
|
66.3
|
1.0
|
C13
|
F:B13500
|
4.3
|
66.0
|
1.0
|
C7
|
F:B13500
|
4.3
|
68.6
|
1.0
|
C26
|
F:B13500
|
4.6
|
63.3
|
1.0
|
ND1
|
F:HIS136
|
4.7
|
58.2
|
1.0
|
C37
|
F:B13500
|
4.7
|
69.7
|
1.0
|
CG
|
F:HIS136
|
4.8
|
58.7
|
1.0
|
C54
|
F:B13500
|
4.9
|
64.2
|
1.0
|
C35
|
F:B13500
|
4.9
|
66.2
|
1.0
|
C53
|
F:B13500
|
4.9
|
64.5
|
1.0
|
C46
|
F:B13500
|
5.0
|
66.7
|
1.0
|
|
Cobalt binding site 4 out
of 8 in 2i2x
Go back to
Cobalt Binding Sites List in 2i2x
Cobalt binding site 4 out
of 8 in the Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 4 of Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Co500
b:54.1
occ:1.00
|
CO
|
H:B13500
|
0.0
|
54.1
|
1.0
|
N24
|
H:B13500
|
1.8
|
54.4
|
1.0
|
N21
|
H:B13500
|
1.8
|
53.3
|
1.0
|
N22
|
H:B13500
|
1.9
|
55.4
|
1.0
|
N23
|
H:B13500
|
1.9
|
54.4
|
1.0
|
NE2
|
H:HIS136
|
2.6
|
57.5
|
1.0
|
C19
|
H:B13500
|
2.8
|
54.2
|
1.0
|
C1
|
H:B13500
|
2.8
|
53.4
|
1.0
|
C9
|
H:B13500
|
2.8
|
56.2
|
1.0
|
C11
|
H:B13500
|
2.9
|
55.4
|
1.0
|
C4
|
H:B13500
|
2.9
|
53.3
|
1.0
|
C16
|
H:B13500
|
2.9
|
54.9
|
1.0
|
C14
|
H:B13500
|
3.0
|
55.2
|
1.0
|
C6
|
H:B13500
|
3.0
|
56.4
|
1.0
|
C10
|
H:B13500
|
3.2
|
55.6
|
1.0
|
CE1
|
H:HIS136
|
3.4
|
57.0
|
1.0
|
C5
|
H:B13500
|
3.4
|
55.2
|
1.0
|
C20
|
H:B13500
|
3.4
|
53.0
|
1.0
|
C15
|
H:B13500
|
3.4
|
54.4
|
1.0
|
O
|
H:HOH501
|
3.6
|
18.1
|
0.5
|
CD2
|
H:HIS136
|
3.7
|
57.8
|
1.0
|
C18
|
H:B13500
|
4.1
|
55.1
|
1.0
|
C2
|
H:B13500
|
4.1
|
52.7
|
1.0
|
C3
|
H:B13500
|
4.2
|
51.8
|
1.0
|
C8
|
H:B13500
|
4.2
|
58.2
|
1.0
|
C17
|
H:B13500
|
4.2
|
55.0
|
1.0
|
C12
|
H:B13500
|
4.2
|
56.1
|
1.0
|
C13
|
H:B13500
|
4.3
|
56.5
|
1.0
|
C7
|
H:B13500
|
4.3
|
58.4
|
1.0
|
ND1
|
H:HIS136
|
4.6
|
57.9
|
1.0
|
C26
|
H:B13500
|
4.6
|
53.0
|
1.0
|
CG
|
H:HIS136
|
4.8
|
58.5
|
1.0
|
C37
|
H:B13500
|
4.9
|
59.3
|
1.0
|
C46
|
H:B13500
|
4.9
|
56.0
|
1.0
|
C35
|
H:B13500
|
4.9
|
56.1
|
1.0
|
C54
|
H:B13500
|
4.9
|
55.5
|
1.0
|
C41
|
H:B13500
|
4.9
|
59.8
|
1.0
|
C53
|
H:B13500
|
4.9
|
52.2
|
1.0
|
|
Cobalt binding site 5 out
of 8 in 2i2x
Go back to
Cobalt Binding Sites List in 2i2x
Cobalt binding site 5 out
of 8 in the Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 5 of Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
J:Co500
b:32.8
occ:1.00
|
CO
|
J:B13500
|
0.0
|
32.8
|
1.0
|
N24
|
J:B13500
|
1.8
|
33.0
|
1.0
|
N21
|
J:B13500
|
1.9
|
34.1
|
1.0
|
N22
|
J:B13500
|
1.9
|
38.3
|
1.0
|
N23
|
J:B13500
|
1.9
|
34.7
|
1.0
|
NE2
|
J:HIS136
|
2.4
|
43.0
|
1.0
|
C19
|
J:B13500
|
2.8
|
33.9
|
1.0
|
C9
|
J:B13500
|
2.8
|
40.1
|
1.0
|
C1
|
J:B13500
|
2.9
|
34.4
|
1.0
|
C11
|
J:B13500
|
2.9
|
35.8
|
1.0
|
C4
|
J:B13500
|
2.9
|
35.4
|
1.0
|
C16
|
J:B13500
|
2.9
|
33.7
|
1.0
|
C6
|
J:B13500
|
3.0
|
40.6
|
1.0
|
C14
|
J:B13500
|
3.0
|
34.2
|
1.0
|
O
|
J:HOH501
|
3.1
|
2.8
|
0.5
|
C10
|
J:B13500
|
3.2
|
36.9
|
1.0
|
CE1
|
J:HIS136
|
3.3
|
43.3
|
1.0
|
C5
|
J:B13500
|
3.4
|
38.1
|
1.0
|
CD2
|
J:HIS136
|
3.4
|
44.2
|
1.0
|
C15
|
J:B13500
|
3.4
|
32.9
|
1.0
|
C20
|
J:B13500
|
3.5
|
32.3
|
1.0
|
C18
|
J:B13500
|
4.1
|
34.8
|
1.0
|
C2
|
J:B13500
|
4.1
|
35.8
|
1.0
|
C8
|
J:B13500
|
4.1
|
44.1
|
1.0
|
C17
|
J:B13500
|
4.2
|
34.0
|
1.0
|
C3
|
J:B13500
|
4.2
|
35.9
|
1.0
|
C12
|
J:B13500
|
4.3
|
35.9
|
1.0
|
C13
|
J:B13500
|
4.3
|
35.9
|
1.0
|
C7
|
J:B13500
|
4.3
|
44.1
|
1.0
|
ND1
|
J:HIS136
|
4.5
|
45.5
|
1.0
|
C26
|
J:B13500
|
4.5
|
35.5
|
1.0
|
CG
|
J:HIS136
|
4.5
|
46.4
|
1.0
|
C41
|
J:B13500
|
4.7
|
48.7
|
1.0
|
C37
|
J:B13500
|
4.8
|
46.6
|
1.0
|
C54
|
J:B13500
|
4.8
|
32.9
|
1.0
|
C46
|
J:B13500
|
4.9
|
34.2
|
1.0
|
C35
|
J:B13500
|
4.9
|
36.8
|
1.0
|
C53
|
J:B13500
|
4.9
|
32.2
|
1.0
|
C48
|
J:B13500
|
5.0
|
38.2
|
1.0
|
|
Cobalt binding site 6 out
of 8 in 2i2x
Go back to
Cobalt Binding Sites List in 2i2x
Cobalt binding site 6 out
of 8 in the Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 6 of Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
L:Co500
b:43.5
occ:1.00
|
CO
|
L:B13500
|
0.0
|
43.5
|
1.0
|
N24
|
L:B13500
|
1.8
|
45.5
|
1.0
|
N21
|
L:B13500
|
1.9
|
45.5
|
1.0
|
N22
|
L:B13500
|
1.9
|
47.3
|
1.0
|
N23
|
L:B13500
|
1.9
|
46.7
|
1.0
|
NE2
|
L:HIS136
|
2.6
|
53.2
|
1.0
|
C19
|
L:B13500
|
2.8
|
45.2
|
1.0
|
C9
|
L:B13500
|
2.8
|
48.4
|
1.0
|
O
|
L:HOH501
|
2.8
|
18.9
|
0.5
|
C1
|
L:B13500
|
2.9
|
44.2
|
1.0
|
C11
|
L:B13500
|
2.9
|
47.2
|
1.0
|
C4
|
L:B13500
|
2.9
|
45.4
|
1.0
|
C16
|
L:B13500
|
2.9
|
46.2
|
1.0
|
C6
|
L:B13500
|
3.0
|
48.6
|
1.0
|
C14
|
L:B13500
|
3.0
|
46.5
|
1.0
|
C10
|
L:B13500
|
3.2
|
47.3
|
1.0
|
C5
|
L:B13500
|
3.4
|
47.8
|
1.0
|
CD2
|
L:HIS136
|
3.4
|
54.4
|
1.0
|
C15
|
L:B13500
|
3.5
|
46.0
|
1.0
|
C20
|
L:B13500
|
3.5
|
42.2
|
1.0
|
CE1
|
L:HIS136
|
3.6
|
53.8
|
1.0
|
C18
|
L:B13500
|
4.1
|
46.2
|
1.0
|
C2
|
L:B13500
|
4.1
|
43.9
|
1.0
|
C8
|
L:B13500
|
4.2
|
49.7
|
1.0
|
C3
|
L:B13500
|
4.2
|
44.9
|
1.0
|
C17
|
L:B13500
|
4.2
|
46.9
|
1.0
|
C12
|
L:B13500
|
4.3
|
47.0
|
1.0
|
C7
|
L:B13500
|
4.3
|
49.7
|
1.0
|
C13
|
L:B13500
|
4.3
|
47.5
|
1.0
|
C26
|
L:B13500
|
4.4
|
43.2
|
1.0
|
CG
|
L:HIS136
|
4.6
|
55.2
|
1.0
|
ND1
|
L:HIS136
|
4.7
|
54.7
|
1.0
|
C41
|
L:B13500
|
4.8
|
50.8
|
1.0
|
C54
|
L:B13500
|
4.9
|
46.7
|
1.0
|
C35
|
L:B13500
|
4.9
|
47.6
|
1.0
|
C37
|
L:B13500
|
4.9
|
52.1
|
1.0
|
C46
|
L:B13500
|
4.9
|
46.1
|
1.0
|
C53
|
L:B13500
|
5.0
|
44.7
|
1.0
|
|
Cobalt binding site 7 out
of 8 in 2i2x
Go back to
Cobalt Binding Sites List in 2i2x
Cobalt binding site 7 out
of 8 in the Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 7 of Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
N:Co500
b:65.7
occ:1.00
|
CO
|
N:B13500
|
0.0
|
65.7
|
1.0
|
N21
|
N:B13500
|
1.8
|
65.7
|
1.0
|
N24
|
N:B13500
|
1.8
|
65.5
|
1.0
|
N22
|
N:B13500
|
1.9
|
67.5
|
1.0
|
N23
|
N:B13500
|
1.9
|
66.3
|
1.0
|
NE2
|
N:HIS136
|
2.5
|
57.2
|
1.0
|
C19
|
N:B13500
|
2.8
|
64.6
|
1.0
|
C9
|
N:B13500
|
2.8
|
67.8
|
1.0
|
C1
|
N:B13500
|
2.8
|
64.8
|
1.0
|
C11
|
N:B13500
|
2.9
|
66.9
|
1.0
|
C4
|
N:B13500
|
2.9
|
65.8
|
1.0
|
C16
|
N:B13500
|
3.0
|
64.5
|
1.0
|
C6
|
N:B13500
|
3.0
|
68.3
|
1.0
|
C14
|
N:B13500
|
3.0
|
65.6
|
1.0
|
C10
|
N:B13500
|
3.2
|
67.0
|
1.0
|
O
|
N:HOH501
|
3.3
|
10.9
|
0.5
|
C5
|
N:B13500
|
3.4
|
67.1
|
1.0
|
CD2
|
N:HIS136
|
3.4
|
57.9
|
1.0
|
C20
|
N:B13500
|
3.4
|
63.6
|
1.0
|
C15
|
N:B13500
|
3.5
|
64.8
|
1.0
|
CE1
|
N:HIS136
|
3.5
|
57.4
|
1.0
|
C18
|
N:B13500
|
4.1
|
64.0
|
1.0
|
C2
|
N:B13500
|
4.1
|
64.6
|
1.0
|
C8
|
N:B13500
|
4.2
|
69.2
|
1.0
|
C3
|
N:B13500
|
4.2
|
65.1
|
1.0
|
C12
|
N:B13500
|
4.2
|
66.6
|
1.0
|
C17
|
N:B13500
|
4.2
|
63.7
|
1.0
|
C13
|
N:B13500
|
4.3
|
66.1
|
1.0
|
C7
|
N:B13500
|
4.3
|
69.4
|
1.0
|
C26
|
N:B13500
|
4.6
|
64.3
|
1.0
|
ND1
|
N:HIS136
|
4.6
|
57.9
|
1.0
|
CG
|
N:HIS136
|
4.6
|
58.9
|
1.0
|
C46
|
N:B13500
|
4.6
|
66.3
|
1.0
|
C37
|
N:B13500
|
4.9
|
70.8
|
1.0
|
C35
|
N:B13500
|
4.9
|
66.4
|
1.0
|
C54
|
N:B13500
|
4.9
|
63.7
|
1.0
|
C41
|
N:B13500
|
4.9
|
70.2
|
1.0
|
C48
|
N:B13500
|
5.0
|
65.7
|
1.0
|
C53
|
N:B13500
|
5.0
|
63.8
|
1.0
|
|
Cobalt binding site 8 out
of 8 in 2i2x
Go back to
Cobalt Binding Sites List in 2i2x
Cobalt binding site 8 out
of 8 in the Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 8 of Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
P:Co500
b:37.6
occ:1.00
|
CO
|
P:B13500
|
0.0
|
37.6
|
1.0
|
N24
|
P:B13500
|
1.8
|
36.0
|
1.0
|
N21
|
P:B13500
|
1.8
|
36.8
|
1.0
|
N22
|
P:B13500
|
1.9
|
37.0
|
1.0
|
N23
|
P:B13500
|
1.9
|
36.1
|
1.0
|
NE2
|
P:HIS136
|
2.5
|
46.1
|
1.0
|
C19
|
P:B13500
|
2.8
|
36.9
|
1.0
|
C9
|
P:B13500
|
2.8
|
38.4
|
1.0
|
C1
|
P:B13500
|
2.8
|
37.0
|
1.0
|
C11
|
P:B13500
|
2.9
|
35.9
|
1.0
|
C4
|
P:B13500
|
2.9
|
36.5
|
1.0
|
C16
|
P:B13500
|
2.9
|
36.9
|
1.0
|
C6
|
P:B13500
|
3.0
|
39.5
|
1.0
|
C14
|
P:B13500
|
3.0
|
35.9
|
1.0
|
C10
|
P:B13500
|
3.2
|
36.3
|
1.0
|
CD2
|
P:HIS136
|
3.3
|
46.1
|
1.0
|
C5
|
P:B13500
|
3.4
|
38.2
|
1.0
|
C20
|
P:B13500
|
3.4
|
35.3
|
1.0
|
C15
|
P:B13500
|
3.4
|
35.3
|
1.0
|
O
|
P:HOH501
|
3.5
|
2.0
|
0.5
|
CE1
|
P:HIS136
|
3.6
|
45.9
|
1.0
|
C18
|
P:B13500
|
4.1
|
37.9
|
1.0
|
C2
|
P:B13500
|
4.1
|
37.0
|
1.0
|
C8
|
P:B13500
|
4.2
|
40.9
|
1.0
|
C3
|
P:B13500
|
4.2
|
36.0
|
1.0
|
C17
|
P:B13500
|
4.2
|
37.3
|
1.0
|
C12
|
P:B13500
|
4.3
|
36.6
|
1.0
|
C13
|
P:B13500
|
4.3
|
37.9
|
1.0
|
C7
|
P:B13500
|
4.3
|
41.8
|
1.0
|
CG
|
P:HIS136
|
4.5
|
47.8
|
1.0
|
C26
|
P:B13500
|
4.6
|
37.4
|
1.0
|
ND1
|
P:HIS136
|
4.6
|
47.0
|
1.0
|
C35
|
P:B13500
|
4.9
|
37.7
|
1.0
|
C37
|
P:B13500
|
4.9
|
45.5
|
1.0
|
C41
|
P:B13500
|
4.9
|
43.2
|
1.0
|
C53
|
P:B13500
|
5.0
|
33.5
|
1.0
|
C46
|
P:B13500
|
5.0
|
35.7
|
1.0
|
|
Reference:
C.H.Hagemeier,
M.Krer,
R.K.Thauer,
E.Warkentin,
U.Ermler.
Insight Into the Mechanism of Biological Methanol Activation Based on the Crystal Structure of the Methanol-Cobalamin Methyltransferase Complex Proc.Natl.Acad.Sci.Usa V. 103 18917 2006.
ISSN: ISSN 0027-8424
PubMed: 17142327
DOI: 10.1073/PNAS.0603650103
Page generated: Tue Jul 30 15:15:49 2024
|