Cobalt in PDB 7ruv: Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin
Enzymatic activity of Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin
All present enzymatic activity of Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin:
2.5.1.17;
Protein crystallography data
The structure of Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin, PDB code: 7ruv
was solved by
R.Mascarenhas,
H.Gouda,
M.Koutmos,
R.Banerjee,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
33.00 /
2.10
|
Space group
|
H 3
|
Cell size a, b, c (Å), α, β, γ (°)
|
121.181,
121.181,
169.77,
90,
90,
120
|
R / Rfree (%)
|
18.5 /
21.7
|
Other elements in 7ruv:
The structure of Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin also contains other interesting chemical elements:
Cobalt Binding Sites:
The binding sites of Cobalt atom in the Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin
(pdb code 7ruv). This binding sites where shown within
5.0 Angstroms radius around Cobalt atom.
In total 4 binding sites of Cobalt where determined in the
Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin, PDB code: 7ruv:
Jump to Cobalt binding site number:
1;
2;
3;
4;
Cobalt binding site 1 out
of 4 in 7ruv
Go back to
Cobalt Binding Sites List in 7ruv
Cobalt binding site 1 out
of 4 in the Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 1 of Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Co303
b:38.5
occ:1.00
|
CO
|
A:B12303
|
0.0
|
38.5
|
1.0
|
N23
|
A:B12303
|
1.9
|
39.9
|
1.0
|
N21
|
A:B12303
|
1.9
|
41.1
|
1.0
|
N24
|
A:B12303
|
1.9
|
44.5
|
1.0
|
N22
|
A:B12303
|
1.9
|
42.0
|
1.0
|
C5'
|
A:5AD304
|
2.0
|
39.1
|
1.0
|
C1
|
A:B12303
|
2.8
|
37.8
|
1.0
|
C11
|
A:B12303
|
2.8
|
37.5
|
1.0
|
C9
|
A:B12303
|
2.9
|
39.8
|
1.0
|
C19
|
A:B12303
|
2.9
|
39.3
|
1.0
|
C4
|
A:B12303
|
2.9
|
43.4
|
1.0
|
C16
|
A:B12303
|
2.9
|
41.8
|
1.0
|
C14
|
A:B12303
|
2.9
|
39.9
|
1.0
|
C6
|
A:B12303
|
3.0
|
42.9
|
1.0
|
C4'
|
A:5AD304
|
3.1
|
44.7
|
1.0
|
C10
|
A:B12303
|
3.2
|
35.5
|
1.0
|
C5
|
A:B12303
|
3.4
|
44.2
|
1.0
|
C15
|
A:B12303
|
3.4
|
41.3
|
1.0
|
C20
|
A:B12303
|
3.5
|
39.0
|
1.0
|
CE1
|
A:PHE170
|
3.6
|
41.0
|
1.0
|
CZ
|
A:PHE170
|
3.9
|
38.8
|
1.0
|
O4'
|
A:5AD304
|
4.0
|
43.6
|
1.0
|
C18
|
A:B12303
|
4.1
|
39.3
|
1.0
|
C2
|
A:B12303
|
4.1
|
42.1
|
1.0
|
C17
|
A:B12303
|
4.2
|
42.6
|
1.0
|
C12
|
A:B12303
|
4.2
|
39.7
|
1.0
|
C8
|
A:B12303
|
4.2
|
38.6
|
1.0
|
C3
|
A:B12303
|
4.2
|
37.8
|
1.0
|
C13
|
A:B12303
|
4.2
|
41.6
|
1.0
|
C7
|
A:B12303
|
4.3
|
36.4
|
1.0
|
C3'
|
A:5AD304
|
4.3
|
43.0
|
1.0
|
C26
|
A:B12303
|
4.5
|
39.8
|
1.0
|
O3'
|
A:5AD304
|
4.5
|
49.4
|
1.0
|
CD1
|
A:PHE170
|
4.8
|
41.3
|
1.0
|
C49
|
A:B12303
|
4.8
|
37.4
|
1.0
|
C41
|
A:B12303
|
4.8
|
37.8
|
1.0
|
C37
|
A:B12303
|
4.8
|
38.5
|
1.0
|
C35
|
A:B12303
|
4.9
|
39.3
|
1.0
|
C46
|
A:B12303
|
4.9
|
37.3
|
1.0
|
C54
|
A:B12303
|
4.9
|
42.3
|
1.0
|
C53
|
A:B12303
|
4.9
|
40.5
|
1.0
|
|
Cobalt binding site 2 out
of 4 in 7ruv
Go back to
Cobalt Binding Sites List in 7ruv
Cobalt binding site 2 out
of 4 in the Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 2 of Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Co301
b:35.6
occ:1.00
|
CO
|
B:B12301
|
0.0
|
35.6
|
1.0
|
N23
|
B:B12301
|
1.9
|
40.1
|
1.0
|
N21
|
B:B12301
|
1.9
|
41.7
|
1.0
|
N24
|
B:B12301
|
1.9
|
40.2
|
1.0
|
N22
|
B:B12301
|
1.9
|
39.0
|
1.0
|
C5'
|
B:5AD302
|
2.1
|
32.1
|
1.0
|
C19
|
B:B12301
|
2.8
|
37.6
|
1.0
|
C11
|
B:B12301
|
2.9
|
35.5
|
1.0
|
C9
|
B:B12301
|
2.9
|
37.9
|
1.0
|
C1
|
B:B12301
|
2.9
|
36.9
|
1.0
|
C16
|
B:B12301
|
2.9
|
41.7
|
1.0
|
C4
|
B:B12301
|
2.9
|
38.3
|
1.0
|
C14
|
B:B12301
|
2.9
|
40.5
|
1.0
|
C6
|
B:B12301
|
3.0
|
37.5
|
1.0
|
C4'
|
B:5AD302
|
3.1
|
42.5
|
1.0
|
C10
|
B:B12301
|
3.2
|
33.2
|
1.0
|
C15
|
B:B12301
|
3.4
|
40.3
|
1.0
|
C5
|
B:B12301
|
3.4
|
38.9
|
1.0
|
C20
|
B:B12301
|
3.5
|
35.0
|
1.0
|
CE1
|
B:PHE170
|
3.8
|
38.8
|
1.0
|
O4'
|
B:5AD302
|
3.9
|
40.7
|
1.0
|
C18
|
B:B12301
|
4.1
|
38.4
|
1.0
|
C2
|
B:B12301
|
4.1
|
39.5
|
1.0
|
C17
|
B:B12301
|
4.2
|
40.8
|
1.0
|
C12
|
B:B12301
|
4.2
|
38.6
|
1.0
|
C3
|
B:B12301
|
4.2
|
39.5
|
1.0
|
C8
|
B:B12301
|
4.2
|
35.1
|
1.0
|
C13
|
B:B12301
|
4.2
|
37.3
|
1.0
|
CZ
|
B:PHE170
|
4.3
|
41.0
|
1.0
|
C7
|
B:B12301
|
4.3
|
38.1
|
1.0
|
C3'
|
B:5AD302
|
4.3
|
40.3
|
1.0
|
C26
|
B:B12301
|
4.5
|
39.2
|
1.0
|
O3'
|
B:5AD302
|
4.5
|
44.4
|
1.0
|
C49
|
B:B12301
|
4.7
|
41.5
|
1.0
|
C37
|
B:B12301
|
4.8
|
33.1
|
1.0
|
C35
|
B:B12301
|
4.9
|
38.1
|
1.0
|
C54
|
B:B12301
|
4.9
|
36.6
|
1.0
|
C46
|
B:B12301
|
4.9
|
35.7
|
1.0
|
C53
|
B:B12301
|
4.9
|
35.7
|
1.0
|
C41
|
B:B12301
|
4.9
|
37.9
|
1.0
|
CD1
|
B:PHE170
|
5.0
|
40.1
|
1.0
|
|
Cobalt binding site 3 out
of 4 in 7ruv
Go back to
Cobalt Binding Sites List in 7ruv
Cobalt binding site 3 out
of 4 in the Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 3 of Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Co503
b:37.3
occ:1.00
|
CO
|
C:B12503
|
0.0
|
37.3
|
1.0
|
N23
|
C:B12503
|
1.8
|
36.5
|
1.0
|
N21
|
C:B12503
|
1.8
|
36.8
|
1.0
|
N24
|
C:B12503
|
1.9
|
38.2
|
1.0
|
N22
|
C:B12503
|
1.9
|
36.4
|
1.0
|
C5'
|
C:5AD504
|
2.1
|
35.7
|
1.0
|
C1
|
C:B12503
|
2.8
|
39.5
|
1.0
|
C11
|
C:B12503
|
2.8
|
36.7
|
1.0
|
C9
|
C:B12503
|
2.9
|
34.4
|
1.0
|
C19
|
C:B12503
|
2.9
|
35.4
|
1.0
|
C4
|
C:B12503
|
2.9
|
36.4
|
1.0
|
C14
|
C:B12503
|
2.9
|
37.5
|
1.0
|
C16
|
C:B12503
|
2.9
|
38.5
|
1.0
|
C6
|
C:B12503
|
3.0
|
36.5
|
1.0
|
C4'
|
C:5AD504
|
3.2
|
41.0
|
1.0
|
C10
|
C:B12503
|
3.2
|
35.4
|
1.0
|
C5
|
C:B12503
|
3.4
|
36.0
|
1.0
|
C15
|
C:B12503
|
3.4
|
39.4
|
1.0
|
C20
|
C:B12503
|
3.5
|
37.9
|
1.0
|
CE1
|
C:PHE170
|
3.5
|
40.9
|
1.0
|
CZ
|
C:PHE170
|
3.7
|
41.6
|
1.0
|
O4'
|
C:5AD504
|
4.0
|
38.7
|
1.0
|
C2
|
C:B12503
|
4.1
|
39.1
|
1.0
|
C18
|
C:B12503
|
4.1
|
39.0
|
1.0
|
C3
|
C:B12503
|
4.2
|
35.1
|
1.0
|
C17
|
C:B12503
|
4.2
|
38.8
|
1.0
|
C12
|
C:B12503
|
4.2
|
37.4
|
1.0
|
C13
|
C:B12503
|
4.2
|
37.6
|
1.0
|
C8
|
C:B12503
|
4.2
|
32.7
|
1.0
|
C7
|
C:B12503
|
4.3
|
38.7
|
1.0
|
C3'
|
C:5AD504
|
4.4
|
42.1
|
1.0
|
C26
|
C:B12503
|
4.4
|
36.1
|
1.0
|
O3'
|
C:5AD504
|
4.6
|
42.0
|
1.0
|
C37
|
C:B12503
|
4.8
|
37.1
|
1.0
|
C49
|
C:B12503
|
4.8
|
38.3
|
1.0
|
CD1
|
C:PHE170
|
4.8
|
36.6
|
1.0
|
C35
|
C:B12503
|
4.9
|
32.3
|
1.0
|
C46
|
C:B12503
|
4.9
|
39.4
|
1.0
|
C41
|
C:B12503
|
4.9
|
37.3
|
1.0
|
O
|
C:HOH622
|
4.9
|
45.3
|
1.0
|
C53
|
C:B12503
|
4.9
|
38.7
|
1.0
|
C54
|
C:B12503
|
5.0
|
35.7
|
1.0
|
|
Cobalt binding site 4 out
of 4 in 7ruv
Go back to
Cobalt Binding Sites List in 7ruv
Cobalt binding site 4 out
of 4 in the Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 4 of Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Co301
b:53.3
occ:1.00
|
CO
|
D:B12301
|
0.0
|
53.3
|
1.0
|
N23
|
D:B12301
|
1.8
|
52.1
|
1.0
|
N21
|
D:B12301
|
1.9
|
54.9
|
1.0
|
N24
|
D:B12301
|
1.9
|
57.2
|
1.0
|
N22
|
D:B12301
|
1.9
|
55.5
|
1.0
|
C5'
|
D:5AD302
|
2.2
|
57.1
|
1.0
|
C11
|
D:B12301
|
2.8
|
55.8
|
1.0
|
C9
|
D:B12301
|
2.9
|
52.3
|
1.0
|
C1
|
D:B12301
|
2.9
|
58.2
|
1.0
|
C14
|
D:B12301
|
2.9
|
59.1
|
1.0
|
C19
|
D:B12301
|
2.9
|
57.9
|
1.0
|
C4
|
D:B12301
|
2.9
|
57.4
|
1.0
|
C16
|
D:B12301
|
2.9
|
55.6
|
1.0
|
C6
|
D:B12301
|
3.0
|
51.2
|
1.0
|
C4'
|
D:5AD302
|
3.2
|
60.4
|
1.0
|
C10
|
D:B12301
|
3.2
|
44.1
|
1.0
|
C5
|
D:B12301
|
3.4
|
56.3
|
1.0
|
C15
|
D:B12301
|
3.4
|
56.7
|
1.0
|
C20
|
D:B12301
|
3.5
|
60.1
|
1.0
|
CE1
|
D:PHE170
|
3.5
|
54.6
|
1.0
|
CZ
|
D:PHE170
|
3.8
|
54.6
|
1.0
|
O4'
|
D:5AD302
|
3.9
|
63.0
|
1.0
|
C18
|
D:B12301
|
4.1
|
59.9
|
1.0
|
C2
|
D:B12301
|
4.1
|
60.8
|
1.0
|
C12
|
D:B12301
|
4.2
|
52.3
|
1.0
|
C17
|
D:B12301
|
4.2
|
58.7
|
1.0
|
C13
|
D:B12301
|
4.2
|
53.0
|
1.0
|
C3
|
D:B12301
|
4.2
|
57.1
|
1.0
|
C8
|
D:B12301
|
4.2
|
47.9
|
1.0
|
C7
|
D:B12301
|
4.3
|
46.8
|
1.0
|
C3'
|
D:5AD302
|
4.5
|
60.8
|
1.0
|
C26
|
D:B12301
|
4.5
|
61.5
|
1.0
|
C37
|
D:B12301
|
4.8
|
49.4
|
1.0
|
C35
|
D:B12301
|
4.8
|
52.4
|
1.0
|
CD1
|
D:PHE170
|
4.8
|
50.5
|
1.0
|
C49
|
D:B12301
|
4.8
|
52.8
|
1.0
|
O3'
|
D:5AD302
|
4.8
|
62.7
|
1.0
|
C46
|
D:B12301
|
4.8
|
54.6
|
1.0
|
C41
|
D:B12301
|
4.9
|
44.2
|
1.0
|
C53
|
D:B12301
|
4.9
|
57.1
|
1.0
|
C54
|
D:B12301
|
4.9
|
58.2
|
1.0
|
|
Reference:
H.Gouda,
R.Mascarenhas,
S.Pillay,
M.Ruetz,
M.Koutmos,
R.Banerjee.
Patient Mutations in Human Atp:Cob(I)Alamin Adenosyltransferase Differentially Affect Its Catalytic Versus Chaperone Functions. J.Biol.Chem. 01373 2021.
ISSN: ESSN 1083-351X
PubMed: 34757128
DOI: 10.1016/J.JBC.2021.101373
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