Cobalt in PDB 8q4h: A Membrane-Bound Menaquinol:Organohalide Oxidoreductase Complex Rdh Complex
Other elements in 8q4h:
The structure of A Membrane-Bound Menaquinol:Organohalide Oxidoreductase Complex Rdh Complex also contains other interesting chemical elements:
Cobalt Binding Sites:
The binding sites of Cobalt atom in the A Membrane-Bound Menaquinol:Organohalide Oxidoreductase Complex Rdh Complex
(pdb code 8q4h). This binding sites where shown within
5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the
A Membrane-Bound Menaquinol:Organohalide Oxidoreductase Complex Rdh Complex, PDB code: 8q4h:
Jump to Cobalt binding site number:
1;
2;
Cobalt binding site 1 out
of 2 in 8q4h
Go back to
Cobalt Binding Sites List in 8q4h
Cobalt binding site 1 out
of 2 in the A Membrane-Bound Menaquinol:Organohalide Oxidoreductase Complex Rdh Complex
 Mono view
 Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 1 of A Membrane-Bound Menaquinol:Organohalide Oxidoreductase Complex Rdh Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Co602
b:51.1
occ:1.00
|
CO
|
A:COB602
|
0.0
|
51.1
|
1.0
|
N21
|
A:COB602
|
1.8
|
51.7
|
1.0
|
N22
|
A:COB602
|
1.8
|
51.2
|
1.0
|
N24
|
A:COB602
|
1.8
|
50.9
|
1.0
|
N23
|
A:COB602
|
1.8
|
50.3
|
1.0
|
C19
|
A:COB602
|
2.7
|
50.8
|
1.0
|
C4
|
A:COB602
|
2.7
|
51.8
|
1.0
|
C9
|
A:COB602
|
2.8
|
51.2
|
1.0
|
C14
|
A:COB602
|
2.8
|
50.3
|
1.0
|
C11
|
A:COB602
|
2.8
|
50.3
|
1.0
|
C6
|
A:COB602
|
2.9
|
51.6
|
1.0
|
C1
|
A:COB602
|
2.9
|
51.5
|
1.0
|
C16
|
A:COB602
|
2.9
|
50.5
|
1.0
|
C5
|
A:COB602
|
3.2
|
51.6
|
1.0
|
C10
|
A:COB602
|
3.2
|
50.8
|
1.0
|
C15
|
A:COB602
|
3.2
|
50.1
|
1.0
|
CL2
|
A:JYF601
|
3.6
|
0.5
|
1.0
|
C20
|
A:COB602
|
3.8
|
51.4
|
1.0
|
C2
|
A:COB602
|
3.9
|
52.3
|
1.0
|
C3
|
A:COB602
|
4.0
|
52.4
|
1.0
|
C8
|
A:COB602
|
4.1
|
52.0
|
1.0
|
C18
|
A:COB602
|
4.1
|
50.4
|
1.0
|
C13
|
A:COB602
|
4.1
|
50.1
|
1.0
|
C26
|
A:COB602
|
4.1
|
52.7
|
1.0
|
C7
|
A:COB602
|
4.1
|
52.1
|
1.0
|
C12
|
A:COB602
|
4.1
|
50.2
|
1.0
|
C17
|
A:COB602
|
4.2
|
50.3
|
1.0
|
C41
|
A:COB602
|
4.6
|
52.4
|
1.0
|
H1
|
A:JYF601
|
4.6
|
0.5
|
1.0
|
C53
|
A:COB602
|
4.6
|
49.4
|
1.0
|
C35
|
A:COB602
|
4.6
|
51.7
|
1.0
|
C1
|
A:JYF601
|
4.7
|
0.5
|
1.0
|
C37
|
A:COB602
|
4.7
|
52.1
|
1.0
|
OH
|
A:TYR337
|
4.9
|
17.8
|
1.0
|
C47
|
A:COB602
|
4.9
|
50.3
|
1.0
|
C54
|
A:COB602
|
5.0
|
49.8
|
1.0
|
|
Cobalt binding site 2 out
of 2 in 8q4h
Go back to
Cobalt Binding Sites List in 8q4h
Cobalt binding site 2 out
of 2 in the A Membrane-Bound Menaquinol:Organohalide Oxidoreductase Complex Rdh Complex
 Mono view
 Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 2 of A Membrane-Bound Menaquinol:Organohalide Oxidoreductase Complex Rdh Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Co602
b:51.1
occ:1.00
|
CO
|
B:COB602
|
0.0
|
51.1
|
1.0
|
N21
|
B:COB602
|
1.8
|
51.7
|
1.0
|
N23
|
B:COB602
|
1.8
|
50.3
|
1.0
|
N24
|
B:COB602
|
1.8
|
50.9
|
1.0
|
N22
|
B:COB602
|
1.8
|
51.2
|
1.0
|
C19
|
B:COB602
|
2.7
|
50.8
|
1.0
|
C4
|
B:COB602
|
2.7
|
51.8
|
1.0
|
C9
|
B:COB602
|
2.8
|
51.2
|
1.0
|
C14
|
B:COB602
|
2.8
|
50.3
|
1.0
|
C11
|
B:COB602
|
2.8
|
50.3
|
1.0
|
C1
|
B:COB602
|
2.8
|
51.5
|
1.0
|
C6
|
B:COB602
|
2.9
|
51.6
|
1.0
|
C16
|
B:COB602
|
2.9
|
50.5
|
1.0
|
C5
|
B:COB602
|
3.2
|
51.6
|
1.0
|
C10
|
B:COB602
|
3.2
|
50.8
|
1.0
|
C15
|
B:COB602
|
3.2
|
50.1
|
1.0
|
CL1
|
B:JYF601
|
3.7
|
0.5
|
1.0
|
C20
|
B:COB602
|
3.8
|
51.4
|
1.0
|
C2
|
B:COB602
|
3.9
|
52.3
|
1.0
|
C3
|
B:COB602
|
4.0
|
52.4
|
1.0
|
C8
|
B:COB602
|
4.1
|
52.0
|
1.0
|
C18
|
B:COB602
|
4.1
|
50.4
|
1.0
|
C26
|
B:COB602
|
4.1
|
52.7
|
1.0
|
C13
|
B:COB602
|
4.1
|
50.1
|
1.0
|
C12
|
B:COB602
|
4.1
|
50.2
|
1.0
|
C7
|
B:COB602
|
4.2
|
52.1
|
1.0
|
C17
|
B:COB602
|
4.2
|
50.3
|
1.0
|
C41
|
B:COB602
|
4.6
|
52.4
|
1.0
|
C35
|
B:COB602
|
4.6
|
51.7
|
1.0
|
C53
|
B:COB602
|
4.6
|
49.4
|
1.0
|
H2
|
B:JYF601
|
4.8
|
0.5
|
1.0
|
C37
|
B:COB602
|
4.9
|
52.1
|
1.0
|
C2
|
B:JYF601
|
4.9
|
0.5
|
1.0
|
C47
|
B:COB602
|
5.0
|
50.3
|
1.0
|
C54
|
B:COB602
|
5.0
|
49.8
|
1.0
|
C48
|
B:COB602
|
5.0
|
50.0
|
1.0
|
OH
|
B:TYR337
|
5.0
|
17.0
|
1.0
|
|
Reference:
N.Dongchun,
B.Ekundayo,
S.Henning,
M.Julien,
C.Holliger,
L.Cimmino.
Structure of A Membrane-Bound Menaquinol:Organohalide Oxidoreductase To Be Published.
Page generated: Tue Jul 30 20:00:33 2024
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