Iron in PDB 3mk7: The Structure of CBB3 Cytochrome Oxidase
Protein crystallography data
The structure of The Structure of CBB3 Cytochrome Oxidase, PDB code: 3mk7
was solved by
S.Buschmann,
E.Warkentin,
H.Michel,
U.Ermler,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
15.00 /
3.20
|
|
Space group
|
P 21 21 2
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
136.475,
279.933,
175.192,
90.00,
90.00,
90.00
|
|
R / Rfree (%)
|
18.9 /
22.3
|
Other elements in 3mk7:
The structure of The Structure of CBB3 Cytochrome Oxidase also contains other interesting chemical elements:
Iron Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
20;
Page 3, Binding sites: 21 -
24;
Binding sites:
The binding sites of Iron atom in the The Structure of CBB3 Cytochrome Oxidase
(pdb code 3mk7). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 24 binding sites of Iron where determined in the
The Structure of CBB3 Cytochrome Oxidase, PDB code: 3mk7:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Iron binding site 1 out
of 24 in 3mk7
Go back to
Iron Binding Sites List in 3mk7
Iron binding site 1 out
of 24 in the The Structure of CBB3 Cytochrome Oxidase
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of The Structure of CBB3 Cytochrome Oxidase within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe501
b:56.8
occ:1.00
|
FE
|
A:HEM501
|
0.0
|
56.8
|
1.0
|
|
NE2
|
A:HIS345
|
1.9
|
53.4
|
1.0
|
|
NC
|
A:HEM501
|
2.0
|
56.3
|
1.0
|
|
ND
|
A:HEM501
|
2.0
|
53.2
|
1.0
|
|
NB
|
A:HEM501
|
2.1
|
60.2
|
1.0
|
|
O1
|
A:PEO508
|
2.1
|
57.6
|
1.0
|
|
NA
|
A:HEM501
|
2.1
|
58.1
|
1.0
|
|
CE1
|
A:HIS345
|
2.8
|
55.5
|
1.0
|
|
CD2
|
A:HIS345
|
2.9
|
51.0
|
1.0
|
|
C4C
|
A:HEM501
|
2.9
|
55.9
|
1.0
|
|
C1C
|
A:HEM501
|
3.0
|
59.0
|
1.0
|
|
C1D
|
A:HEM501
|
3.0
|
53.9
|
1.0
|
|
C1B
|
A:HEM501
|
3.0
|
64.2
|
1.0
|
|
C4B
|
A:HEM501
|
3.1
|
62.0
|
1.0
|
|
C4D
|
A:HEM501
|
3.1
|
52.2
|
1.0
|
|
C4A
|
A:HEM501
|
3.1
|
60.0
|
1.0
|
|
C1A
|
A:HEM501
|
3.1
|
55.5
|
1.0
|
|
O2
|
A:PEO508
|
3.3
|
63.8
|
1.0
|
|
CHD
|
A:HEM501
|
3.3
|
55.1
|
1.0
|
|
CHC
|
A:HEM501
|
3.4
|
62.0
|
1.0
|
|
CHB
|
A:HEM501
|
3.4
|
64.8
|
1.0
|
|
CHA
|
A:HEM501
|
3.5
|
54.0
|
1.0
|
|
ND1
|
A:HIS345
|
4.0
|
54.5
|
1.0
|
|
CG
|
A:HIS345
|
4.0
|
52.3
|
1.0
|
|
C3C
|
A:HEM501
|
4.1
|
59.1
|
1.0
|
|
C2C
|
A:HEM501
|
4.2
|
61.8
|
1.0
|
|
C2D
|
A:HEM501
|
4.2
|
49.8
|
1.0
|
|
C3B
|
A:HEM501
|
4.3
|
61.7
|
1.0
|
|
C2B
|
A:HEM501
|
4.3
|
62.3
|
1.0
|
|
C3D
|
A:HEM501
|
4.3
|
50.3
|
1.0
|
|
C3A
|
A:HEM501
|
4.3
|
59.2
|
1.0
|
|
C2A
|
A:HEM501
|
4.3
|
54.6
|
1.0
|
|
CU
|
A:CU503
|
4.6
|
59.3
|
1.0
|
|
CG2
|
A:VAL210
|
4.8
|
64.5
|
1.0
|
|
Iron binding site 2 out
of 24 in 3mk7
Go back to
Iron Binding Sites List in 3mk7
Iron binding site 2 out
of 24 in the The Structure of CBB3 Cytochrome Oxidase
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of The Structure of CBB3 Cytochrome Oxidase within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:54.3
occ:1.00
|
FE
|
A:HEM502
|
0.0
|
54.3
|
1.0
|
|
NE2
|
A:HIS347
|
1.9
|
47.1
|
1.0
|
|
NE2
|
A:HIS60
|
1.9
|
53.2
|
1.0
|
|
NA
|
A:HEM502
|
2.0
|
48.6
|
1.0
|
|
ND
|
A:HEM502
|
2.0
|
50.5
|
1.0
|
|
NB
|
A:HEM502
|
2.0
|
54.1
|
1.0
|
|
NC
|
A:HEM502
|
2.1
|
52.2
|
1.0
|
|
CE1
|
A:HIS60
|
2.6
|
53.9
|
1.0
|
|
CE1
|
A:HIS347
|
2.8
|
46.9
|
1.0
|
|
CD2
|
A:HIS347
|
2.9
|
46.9
|
1.0
|
|
C4A
|
A:HEM502
|
3.0
|
48.5
|
1.0
|
|
C1B
|
A:HEM502
|
3.0
|
54.1
|
1.0
|
|
C1D
|
A:HEM502
|
3.0
|
52.2
|
1.0
|
|
C4D
|
A:HEM502
|
3.0
|
49.9
|
1.0
|
|
C1A
|
A:HEM502
|
3.0
|
50.1
|
1.0
|
|
CD2
|
A:HIS60
|
3.0
|
51.6
|
1.0
|
|
C4C
|
A:HEM502
|
3.1
|
52.9
|
1.0
|
|
C4B
|
A:HEM502
|
3.1
|
53.9
|
1.0
|
|
C1C
|
A:HEM502
|
3.1
|
55.1
|
1.0
|
|
CHB
|
A:HEM502
|
3.3
|
53.1
|
1.0
|
|
CHA
|
A:HEM502
|
3.4
|
50.0
|
1.0
|
|
CHD
|
A:HEM502
|
3.4
|
52.6
|
1.0
|
|
CHC
|
A:HEM502
|
3.4
|
54.6
|
1.0
|
|
ND1
|
A:HIS60
|
3.8
|
53.5
|
1.0
|
|
ND1
|
A:HIS347
|
3.9
|
46.4
|
1.0
|
|
CG
|
A:HIS347
|
4.0
|
47.9
|
1.0
|
|
CG
|
A:HIS60
|
4.1
|
50.9
|
1.0
|
|
OH
|
A:TYR395
|
4.1
|
54.4
|
1.0
|
|
C3A
|
A:HEM502
|
4.2
|
46.4
|
1.0
|
|
C2D
|
A:HEM502
|
4.2
|
52.9
|
1.0
|
|
C3D
|
A:HEM502
|
4.3
|
50.2
|
1.0
|
|
C2B
|
A:HEM502
|
4.3
|
54.9
|
1.0
|
|
C3B
|
A:HEM502
|
4.3
|
55.8
|
1.0
|
|
C2A
|
A:HEM502
|
4.3
|
48.1
|
1.0
|
|
C3C
|
A:HEM502
|
4.3
|
56.3
|
1.0
|
|
C2C
|
A:HEM502
|
4.3
|
57.1
|
1.0
|
|
Iron binding site 3 out
of 24 in 3mk7
Go back to
Iron Binding Sites List in 3mk7
Iron binding site 3 out
of 24 in the The Structure of CBB3 Cytochrome Oxidase
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of The Structure of CBB3 Cytochrome Oxidase within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe211
b:33.1
occ:1.00
|
FE
|
B:HEC211
|
0.0
|
33.1
|
1.0
|
|
NE2
|
B:HIS69
|
1.9
|
44.3
|
1.0
|
|
NC
|
B:HEC211
|
2.0
|
28.0
|
1.0
|
|
ND
|
B:HEC211
|
2.0
|
25.1
|
1.0
|
|
NA
|
B:HEC211
|
2.0
|
27.5
|
1.0
|
|
NB
|
B:HEC211
|
2.0
|
27.8
|
1.0
|
|
SD
|
B:MET137
|
2.3
|
48.6
|
1.0
|
|
CD2
|
B:HIS69
|
2.8
|
43.5
|
1.0
|
|
CE1
|
B:HIS69
|
2.9
|
43.1
|
1.0
|
|
C1C
|
B:HEC211
|
2.9
|
29.1
|
1.0
|
|
C1A
|
B:HEC211
|
3.0
|
28.2
|
1.0
|
|
C4B
|
B:HEC211
|
3.0
|
30.4
|
1.0
|
|
C4D
|
B:HEC211
|
3.0
|
25.8
|
1.0
|
|
C1D
|
B:HEC211
|
3.0
|
26.8
|
1.0
|
|
C4A
|
B:HEC211
|
3.0
|
27.1
|
1.0
|
|
C4C
|
B:HEC211
|
3.0
|
27.7
|
1.0
|
|
C1B
|
B:HEC211
|
3.1
|
28.1
|
1.0
|
|
CG
|
B:MET137
|
3.2
|
45.9
|
1.0
|
|
CHC
|
B:HEC211
|
3.3
|
30.4
|
1.0
|
|
CHA
|
B:HEC211
|
3.3
|
28.2
|
1.0
|
|
CE
|
B:MET137
|
3.4
|
39.5
|
1.0
|
|
CHD
|
B:HEC211
|
3.4
|
25.6
|
1.0
|
|
CHB
|
B:HEC211
|
3.5
|
27.5
|
1.0
|
|
CB
|
B:MET137
|
4.0
|
43.7
|
1.0
|
|
ND1
|
B:HIS69
|
4.0
|
50.9
|
1.0
|
|
CG
|
B:HIS69
|
4.0
|
45.9
|
1.0
|
|
C2C
|
B:HEC211
|
4.2
|
27.8
|
1.0
|
|
C2A
|
B:HEC211
|
4.2
|
27.1
|
1.0
|
|
C3C
|
B:HEC211
|
4.2
|
30.5
|
1.0
|
|
C3B
|
B:HEC211
|
4.2
|
31.4
|
1.0
|
|
C3D
|
B:HEC211
|
4.2
|
26.6
|
1.0
|
|
C2D
|
B:HEC211
|
4.3
|
27.0
|
1.0
|
|
C3A
|
B:HEC211
|
4.3
|
28.5
|
1.0
|
|
C2B
|
B:HEC211
|
4.3
|
29.4
|
1.0
|
|
CE1
|
B:HIS124
|
4.8
|
53.8
|
1.0
|
|
Iron binding site 4 out
of 24 in 3mk7
Go back to
Iron Binding Sites List in 3mk7
Iron binding site 4 out
of 24 in the The Structure of CBB3 Cytochrome Oxidase
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of The Structure of CBB3 Cytochrome Oxidase within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe321
b:24.9
occ:1.00
|
FE
|
C:HEC321
|
0.0
|
24.9
|
1.0
|
|
NE2
|
C:HIS237
|
1.9
|
51.1
|
1.0
|
|
NA
|
C:HEC321
|
1.9
|
25.3
|
1.0
|
|
NC
|
C:HEC321
|
2.0
|
26.9
|
1.0
|
|
ND
|
C:HEC321
|
2.0
|
27.9
|
1.0
|
|
NB
|
C:HEC321
|
2.0
|
23.6
|
1.0
|
|
SD
|
C:MET186
|
2.3
|
51.4
|
1.0
|
|
CE1
|
C:HIS237
|
2.8
|
52.5
|
1.0
|
|
CG
|
C:MET186
|
2.9
|
48.3
|
1.0
|
|
CD2
|
C:HIS237
|
2.9
|
52.7
|
1.0
|
|
C4A
|
C:HEC321
|
3.0
|
27.1
|
1.0
|
|
C1C
|
C:HEC321
|
3.0
|
29.9
|
1.0
|
|
C1D
|
C:HEC321
|
3.0
|
28.6
|
1.0
|
|
C1A
|
C:HEC321
|
3.0
|
26.0
|
1.0
|
|
C1B
|
C:HEC321
|
3.0
|
24.1
|
1.0
|
|
C4C
|
C:HEC321
|
3.0
|
27.3
|
1.0
|
|
C4D
|
C:HEC321
|
3.0
|
27.3
|
1.0
|
|
C4B
|
C:HEC321
|
3.1
|
23.8
|
1.0
|
|
CE
|
C:MET186
|
3.3
|
50.2
|
1.0
|
|
CHB
|
C:HEC321
|
3.3
|
26.9
|
1.0
|
|
CHD
|
C:HEC321
|
3.4
|
27.6
|
1.0
|
|
CHC
|
C:HEC321
|
3.4
|
26.8
|
1.0
|
|
CHA
|
C:HEC321
|
3.4
|
25.6
|
1.0
|
|
ND1
|
C:HIS237
|
3.9
|
54.0
|
1.0
|
|
CG
|
C:HIS237
|
4.0
|
53.2
|
1.0
|
|
CB
|
C:MET186
|
4.2
|
50.2
|
1.0
|
|
C3A
|
C:HEC321
|
4.2
|
26.5
|
1.0
|
|
C2C
|
C:HEC321
|
4.2
|
29.7
|
1.0
|
|
C2A
|
C:HEC321
|
4.2
|
26.2
|
1.0
|
|
C2D
|
C:HEC321
|
4.3
|
27.7
|
1.0
|
|
C3C
|
C:HEC321
|
4.3
|
28.9
|
1.0
|
|
C3D
|
C:HEC321
|
4.3
|
28.4
|
1.0
|
|
C2B
|
C:HEC321
|
4.3
|
23.5
|
1.0
|
|
C3B
|
C:HEC321
|
4.3
|
23.3
|
1.0
|
|
CA
|
C:MET186
|
4.6
|
49.4
|
1.0
|
|
Iron binding site 5 out
of 24 in 3mk7
Go back to
Iron Binding Sites List in 3mk7
Iron binding site 5 out
of 24 in the The Structure of CBB3 Cytochrome Oxidase
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of The Structure of CBB3 Cytochrome Oxidase within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe322
b:28.6
occ:1.00
|
FE
|
C:HEC322
|
0.0
|
28.6
|
1.0
|
|
NE2
|
C:HIS147
|
1.9
|
49.0
|
1.0
|
|
NA
|
C:HEC322
|
1.9
|
25.7
|
1.0
|
|
NB
|
C:HEC322
|
2.0
|
23.8
|
1.0
|
|
NC
|
C:HEC322
|
2.0
|
28.6
|
1.0
|
|
ND
|
C:HEC322
|
2.0
|
28.6
|
1.0
|
|
SD
|
C:MET279
|
2.2
|
50.1
|
1.0
|
|
CE1
|
C:HIS147
|
2.8
|
49.3
|
1.0
|
|
C4A
|
C:HEC322
|
2.9
|
28.1
|
1.0
|
|
C1A
|
C:HEC322
|
3.0
|
28.5
|
1.0
|
|
CD2
|
C:HIS147
|
3.0
|
48.7
|
1.0
|
|
C1B
|
C:HEC322
|
3.0
|
26.3
|
1.0
|
|
C1D
|
C:HEC322
|
3.0
|
29.8
|
1.0
|
|
C1C
|
C:HEC322
|
3.0
|
33.3
|
1.0
|
|
C4C
|
C:HEC322
|
3.0
|
28.8
|
1.0
|
|
C4B
|
C:HEC322
|
3.0
|
24.2
|
1.0
|
|
C4D
|
C:HEC322
|
3.1
|
29.2
|
1.0
|
|
CG
|
C:MET279
|
3.3
|
52.2
|
1.0
|
|
CHB
|
C:HEC322
|
3.3
|
31.4
|
1.0
|
|
CHA
|
C:HEC322
|
3.4
|
28.6
|
1.0
|
|
CHD
|
C:HEC322
|
3.4
|
28.3
|
1.0
|
|
CE
|
C:MET279
|
3.4
|
53.8
|
1.0
|
|
CHC
|
C:HEC322
|
3.4
|
29.1
|
1.0
|
|
CB
|
C:MET279
|
3.9
|
53.3
|
1.0
|
|
ND1
|
C:HIS147
|
3.9
|
49.3
|
1.0
|
|
CG
|
C:HIS147
|
4.0
|
49.3
|
1.0
|
|
C2A
|
C:HEC322
|
4.2
|
26.0
|
1.0
|
|
C3A
|
C:HEC322
|
4.2
|
25.5
|
1.0
|
|
C2C
|
C:HEC322
|
4.3
|
30.7
|
1.0
|
|
C2B
|
C:HEC322
|
4.3
|
24.3
|
1.0
|
|
C3C
|
C:HEC322
|
4.3
|
32.4
|
1.0
|
|
C3B
|
C:HEC322
|
4.3
|
24.7
|
1.0
|
|
C2D
|
C:HEC322
|
4.3
|
27.8
|
1.0
|
|
C3D
|
C:HEC322
|
4.3
|
27.9
|
1.0
|
|
CA
|
C:MET279
|
4.5
|
51.3
|
1.0
|
|
Iron binding site 6 out
of 24 in 3mk7
Go back to
Iron Binding Sites List in 3mk7
Iron binding site 6 out
of 24 in the The Structure of CBB3 Cytochrome Oxidase
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of The Structure of CBB3 Cytochrome Oxidase within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
M:Fe323
b:28.4
occ:0.75
|
FE2
|
M:FC6323
|
0.0
|
28.4
|
0.8
|
|
C22
|
M:FC6323
|
1.9
|
28.7
|
0.8
|
|
C23
|
M:FC6323
|
1.9
|
30.2
|
0.8
|
|
C11
|
M:FC6323
|
1.9
|
28.1
|
0.8
|
|
C21
|
M:FC6323
|
1.9
|
33.1
|
0.8
|
|
C24
|
M:FC6323
|
1.9
|
36.7
|
0.8
|
|
C26
|
M:FC6323
|
1.9
|
30.3
|
0.8
|
|
N22
|
M:FC6323
|
3.0
|
31.2
|
0.8
|
|
N23
|
M:FC6323
|
3.0
|
36.3
|
0.8
|
|
N11
|
M:FC6323
|
3.0
|
28.3
|
0.8
|
|
N25
|
M:FC6323
|
3.1
|
38.1
|
0.8
|
|
N21
|
M:FC6323
|
3.1
|
28.4
|
0.8
|
|
N24
|
M:FC6323
|
3.1
|
39.4
|
0.8
|
|
CG
|
C:PRO215
|
4.4
|
63.6
|
1.0
|
|
CG
|
M:GLN266
|
4.5
|
45.9
|
1.0
|
|
CB
|
C:PRO215
|
4.8
|
65.2
|
1.0
|
|
NH2
|
C:ARG206
|
4.9
|
63.8
|
1.0
|
|
CB
|
C:SER263
|
5.0
|
59.0
|
1.0
|
|
Iron binding site 7 out
of 24 in 3mk7
Go back to
Iron Binding Sites List in 3mk7
Iron binding site 7 out
of 24 in the The Structure of CBB3 Cytochrome Oxidase
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of The Structure of CBB3 Cytochrome Oxidase within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe501
b:0.8
occ:1.00
|
FE
|
D:HEM501
|
0.0
|
0.8
|
1.0
|
|
NE2
|
D:HIS345
|
1.9
|
0.7
|
1.0
|
|
NA
|
D:HEM501
|
2.0
|
0.3
|
1.0
|
|
NB
|
D:HEM501
|
2.0
|
0.1
|
1.0
|
|
O1
|
D:PEO508
|
2.1
|
0.7
|
1.0
|
|
ND
|
D:HEM501
|
2.1
|
0.1
|
1.0
|
|
NC
|
D:HEM501
|
2.1
|
0.9
|
1.0
|
|
CD2
|
D:HIS345
|
2.9
|
0.7
|
1.0
|
|
CE1
|
D:HIS345
|
2.9
|
0.9
|
1.0
|
|
C4A
|
D:HEM501
|
3.0
|
0.1
|
1.0
|
|
C1B
|
D:HEM501
|
3.0
|
0.3
|
1.0
|
|
C1A
|
D:HEM501
|
3.0
|
0.8
|
1.0
|
|
C4B
|
D:HEM501
|
3.0
|
0.9
|
1.0
|
|
C1D
|
D:HEM501
|
3.1
|
0.7
|
1.0
|
|
C4C
|
D:HEM501
|
3.1
|
0.2
|
1.0
|
|
C4D
|
D:HEM501
|
3.1
|
0.5
|
1.0
|
|
C1C
|
D:HEM501
|
3.1
|
0.6
|
1.0
|
|
O2
|
D:PEO508
|
3.3
|
0.4
|
1.0
|
|
CHB
|
D:HEM501
|
3.4
|
0.9
|
1.0
|
|
CHD
|
D:HEM501
|
3.4
|
0.9
|
1.0
|
|
CHA
|
D:HEM501
|
3.4
|
0.2
|
1.0
|
|
CHC
|
D:HEM501
|
3.4
|
0.9
|
1.0
|
|
ND1
|
D:HIS345
|
4.0
|
0.8
|
1.0
|
|
CG
|
D:HIS345
|
4.0
|
0.2
|
1.0
|
|
C2B
|
D:HEM501
|
4.2
|
0.5
|
1.0
|
|
C3A
|
D:HEM501
|
4.2
|
0.7
|
1.0
|
|
C3B
|
D:HEM501
|
4.2
|
0.3
|
1.0
|
|
C2A
|
D:HEM501
|
4.2
|
0.8
|
1.0
|
|
C2C
|
D:HEM501
|
4.3
|
0.3
|
1.0
|
|
C3C
|
D:HEM501
|
4.3
|
0.5
|
1.0
|
|
C2D
|
D:HEM501
|
4.3
|
0.9
|
1.0
|
|
C3D
|
D:HEM501
|
4.3
|
0.7
|
1.0
|
|
CU
|
D:CU503
|
4.5
|
0.1
|
1.0
|
|
CG2
|
D:VAL210
|
4.8
|
0.8
|
1.0
|
|
ND1
|
D:HIS207
|
4.9
|
0.9
|
1.0
|
|
NE2
|
D:HIS257
|
4.9
|
0.2
|
1.0
|
|
Iron binding site 8 out
of 24 in 3mk7
Go back to
Iron Binding Sites List in 3mk7
Iron binding site 8 out
of 24 in the The Structure of CBB3 Cytochrome Oxidase
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of The Structure of CBB3 Cytochrome Oxidase within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe502
b:97.0
occ:1.00
|
FE
|
D:HEM502
|
0.0
|
97.0
|
1.0
|
|
NE2
|
D:HIS347
|
1.8
|
0.7
|
1.0
|
|
NE2
|
D:HIS60
|
1.9
|
92.0
|
1.0
|
|
NA
|
D:HEM502
|
2.0
|
91.2
|
1.0
|
|
NB
|
D:HEM502
|
2.0
|
99.7
|
1.0
|
|
ND
|
D:HEM502
|
2.0
|
94.7
|
1.0
|
|
NC
|
D:HEM502
|
2.1
|
0.5
|
1.0
|
|
CE1
|
D:HIS60
|
2.7
|
93.3
|
1.0
|
|
CE1
|
D:HIS347
|
2.8
|
0.3
|
1.0
|
|
CD2
|
D:HIS347
|
2.9
|
0.4
|
1.0
|
|
C4A
|
D:HEM502
|
3.0
|
91.1
|
1.0
|
|
C1B
|
D:HEM502
|
3.0
|
98.9
|
1.0
|
|
C4D
|
D:HEM502
|
3.0
|
92.1
|
1.0
|
|
C1D
|
D:HEM502
|
3.0
|
96.1
|
1.0
|
|
C1A
|
D:HEM502
|
3.0
|
88.6
|
1.0
|
|
CD2
|
D:HIS60
|
3.1
|
88.0
|
1.0
|
|
C4B
|
D:HEM502
|
3.1
|
0.8
|
1.0
|
|
C4C
|
D:HEM502
|
3.1
|
0.5
|
1.0
|
|
C1C
|
D:HEM502
|
3.1
|
0.4
|
1.0
|
|
CHB
|
D:HEM502
|
3.4
|
94.6
|
1.0
|
|
CHA
|
D:HEM502
|
3.4
|
89.0
|
1.0
|
|
CHD
|
D:HEM502
|
3.4
|
99.4
|
1.0
|
|
CHC
|
D:HEM502
|
3.4
|
0.9
|
1.0
|
|
ND1
|
D:HIS60
|
3.8
|
92.6
|
1.0
|
|
ND1
|
D:HIS347
|
3.9
|
0.1
|
1.0
|
|
CG
|
D:HIS347
|
4.0
|
0.6
|
1.0
|
|
CG
|
D:HIS60
|
4.1
|
89.5
|
1.0
|
|
OH
|
D:TYR395
|
4.1
|
98.0
|
1.0
|
|
C3A
|
D:HEM502
|
4.2
|
87.8
|
1.0
|
|
C2B
|
D:HEM502
|
4.2
|
0.5
|
1.0
|
|
C3B
|
D:HEM502
|
4.3
|
0.9
|
1.0
|
|
C2D
|
D:HEM502
|
4.3
|
96.0
|
1.0
|
|
C2A
|
D:HEM502
|
4.3
|
87.0
|
1.0
|
|
C3D
|
D:HEM502
|
4.3
|
93.3
|
1.0
|
|
C2C
|
D:HEM502
|
4.3
|
0.1
|
1.0
|
|
C3C
|
D:HEM502
|
4.3
|
0.9
|
1.0
|
|
Iron binding site 9 out
of 24 in 3mk7
Go back to
Iron Binding Sites List in 3mk7
Iron binding site 9 out
of 24 in the The Structure of CBB3 Cytochrome Oxidase
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 9 of The Structure of CBB3 Cytochrome Oxidase within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Fe211
b:19.0
occ:1.00
|
FE
|
E:HEC211
|
0.0
|
19.0
|
1.0
|
|
NE2
|
E:HIS69
|
1.8
|
75.0
|
1.0
|
|
NA
|
E:HEC211
|
1.9
|
18.1
|
1.0
|
|
NB
|
E:HEC211
|
2.0
|
18.4
|
1.0
|
|
NC
|
E:HEC211
|
2.0
|
17.6
|
1.0
|
|
ND
|
E:HEC211
|
2.0
|
17.0
|
1.0
|
|
SD
|
E:MET137
|
2.4
|
72.1
|
1.0
|
|
CD2
|
E:HIS69
|
2.8
|
77.3
|
1.0
|
|
CE1
|
E:HIS69
|
2.9
|
79.7
|
1.0
|
|
C1A
|
E:HEC211
|
2.9
|
18.6
|
1.0
|
|
C4A
|
E:HEC211
|
3.0
|
18.3
|
1.0
|
|
C4B
|
E:HEC211
|
3.0
|
19.2
|
1.0
|
|
C4D
|
E:HEC211
|
3.0
|
17.7
|
1.0
|
|
C1C
|
E:HEC211
|
3.0
|
18.1
|
1.0
|
|
C1B
|
E:HEC211
|
3.1
|
18.8
|
1.0
|
|
C1D
|
E:HEC211
|
3.1
|
17.4
|
1.0
|
|
C4C
|
E:HEC211
|
3.1
|
17.9
|
1.0
|
|
CHA
|
E:HEC211
|
3.3
|
18.1
|
1.0
|
|
CHC
|
E:HEC211
|
3.4
|
18.4
|
1.0
|
|
CG
|
E:MET137
|
3.4
|
64.9
|
1.0
|
|
CHB
|
E:HEC211
|
3.4
|
18.6
|
1.0
|
|
CE
|
E:MET137
|
3.4
|
66.9
|
1.0
|
|
CHD
|
E:HEC211
|
3.5
|
18.2
|
1.0
|
|
ND1
|
E:HIS69
|
4.0
|
82.2
|
1.0
|
|
CG
|
E:HIS69
|
4.0
|
80.7
|
1.0
|
|
CB
|
E:MET137
|
4.0
|
64.1
|
1.0
|
|
C2A
|
E:HEC211
|
4.1
|
18.8
|
1.0
|
|
C3A
|
E:HEC211
|
4.2
|
18.0
|
1.0
|
|
C3B
|
E:HEC211
|
4.2
|
20.8
|
1.0
|
|
C2C
|
E:HEC211
|
4.3
|
18.4
|
1.0
|
|
C2B
|
E:HEC211
|
4.3
|
20.1
|
1.0
|
|
C3D
|
E:HEC211
|
4.3
|
18.6
|
1.0
|
|
C2D
|
E:HEC211
|
4.3
|
17.6
|
1.0
|
|
C3C
|
E:HEC211
|
4.3
|
18.6
|
1.0
|
|
CE1
|
E:HIS124
|
4.8
|
72.8
|
1.0
|
|
Iron binding site 10 out
of 24 in 3mk7
Go back to
Iron Binding Sites List in 3mk7
Iron binding site 10 out
of 24 in the The Structure of CBB3 Cytochrome Oxidase
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 10 of The Structure of CBB3 Cytochrome Oxidase within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Fe321
b:20.3
occ:1.00
|
FE
|
F:HEC321
|
0.0
|
20.3
|
1.0
|
|
NE2
|
F:HIS237
|
1.9
|
81.6
|
1.0
|
|
NA
|
F:HEC321
|
2.0
|
25.9
|
1.0
|
|
NB
|
F:HEC321
|
2.0
|
21.8
|
1.0
|
|
NC
|
F:HEC321
|
2.0
|
24.3
|
1.0
|
|
ND
|
F:HEC321
|
2.1
|
23.4
|
1.0
|
|
SD
|
F:MET186
|
2.3
|
81.2
|
1.0
|
|
CE1
|
F:HIS237
|
2.8
|
81.7
|
1.0
|
|
CD2
|
F:HIS237
|
2.9
|
84.4
|
1.0
|
|
CG
|
F:MET186
|
2.9
|
81.3
|
1.0
|
|
C4A
|
F:HEC321
|
3.0
|
26.5
|
1.0
|
|
C1B
|
F:HEC321
|
3.0
|
23.3
|
1.0
|
|
C4B
|
F:HEC321
|
3.0
|
22.7
|
1.0
|
|
C1C
|
F:HEC321
|
3.0
|
24.2
|
1.0
|
|
C1A
|
F:HEC321
|
3.0
|
27.1
|
1.0
|
|
C4C
|
F:HEC321
|
3.0
|
24.6
|
1.0
|
|
C1D
|
F:HEC321
|
3.1
|
23.2
|
1.0
|
|
C4D
|
F:HEC321
|
3.1
|
24.4
|
1.0
|
|
CHB
|
F:HEC321
|
3.4
|
25.6
|
1.0
|
|
CHD
|
F:HEC321
|
3.4
|
24.4
|
1.0
|
|
CHC
|
F:HEC321
|
3.4
|
25.1
|
1.0
|
|
CHA
|
F:HEC321
|
3.4
|
26.3
|
1.0
|
|
CE
|
F:MET186
|
3.5
|
81.1
|
1.0
|
|
ND1
|
F:HIS237
|
4.0
|
84.1
|
1.0
|
|
CG
|
F:HIS237
|
4.0
|
86.0
|
1.0
|
|
C2C
|
F:HEC321
|
4.2
|
23.4
|
1.0
|
|
C2B
|
F:HEC321
|
4.2
|
23.8
|
1.0
|
|
C3A
|
F:HEC321
|
4.2
|
27.2
|
1.0
|
|
CB
|
F:MET186
|
4.2
|
86.0
|
1.0
|
|
C3B
|
F:HEC321
|
4.2
|
22.8
|
1.0
|
|
C2A
|
F:HEC321
|
4.3
|
27.6
|
1.0
|
|
C3C
|
F:HEC321
|
4.3
|
24.4
|
1.0
|
|
C2D
|
F:HEC321
|
4.3
|
23.0
|
1.0
|
|
C3D
|
F:HEC321
|
4.3
|
23.8
|
1.0
|
|
CA
|
F:MET186
|
4.7
|
93.2
|
1.0
|
|
Reference:
S.Buschmann,
E.Warkentin,
H.Xie,
J.D.Langer,
U.Ermler,
H.Michel.
The Structure of CBB3 Cytochrome Oxidase Provides Insights Into Proton Pumping Science V. 329 327 2010.
ISSN: ISSN 0036-8075
PubMed: 20576851
DOI: 10.1126/SCIENCE.1187303
Page generated: Sun Aug 4 14:50:03 2024
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