Copper in PDB 5z84: The Structure of Azide-Bound Cytochrome C Oxidase Determined Using the Crystals Exposed to 20 Mm Azide Solution For 4 Days
Enzymatic activity of The Structure of Azide-Bound Cytochrome C Oxidase Determined Using the Crystals Exposed to 20 Mm Azide Solution For 4 Days
All present enzymatic activity of The Structure of Azide-Bound Cytochrome C Oxidase Determined Using the Crystals Exposed to 20 Mm Azide Solution For 4 Days:
1.9.3.1;
Protein crystallography data
The structure of The Structure of Azide-Bound Cytochrome C Oxidase Determined Using the Crystals Exposed to 20 Mm Azide Solution For 4 Days, PDB code: 5z84
was solved by
A.Shimada,
K.Hatano,
H.Tadehara,
T.Tsukihara,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
40.00 /
1.85
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
183.405,
206.272,
177.609,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
16.3 /
18.9
|
Other elements in 5z84:
The structure of The Structure of Azide-Bound Cytochrome C Oxidase Determined Using the Crystals Exposed to 20 Mm Azide Solution For 4 Days also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the The Structure of Azide-Bound Cytochrome C Oxidase Determined Using the Crystals Exposed to 20 Mm Azide Solution For 4 Days
(pdb code 5z84). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the
The Structure of Azide-Bound Cytochrome C Oxidase Determined Using the Crystals Exposed to 20 Mm Azide Solution For 4 Days, PDB code: 5z84:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
Copper binding site 1 out
of 6 in 5z84
Go back to
Copper Binding Sites List in 5z84
Copper binding site 1 out
of 6 in the The Structure of Azide-Bound Cytochrome C Oxidase Determined Using the Crystals Exposed to 20 Mm Azide Solution For 4 Days
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of The Structure of Azide-Bound Cytochrome C Oxidase Determined Using the Crystals Exposed to 20 Mm Azide Solution For 4 Days within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu603
b:30.3
occ:1.00
|
N1
|
A:AZI606
|
1.8
|
33.5
|
1.0
|
NE2
|
A:HIS291
|
2.0
|
27.7
|
1.0
|
ND1
|
A:HIS240
|
2.0
|
26.1
|
1.0
|
NE2
|
A:HIS290
|
2.1
|
30.0
|
1.0
|
N2
|
A:AZI606
|
2.7
|
36.7
|
1.0
|
CD2
|
A:HIS291
|
3.0
|
27.0
|
1.0
|
CE1
|
A:HIS291
|
3.0
|
24.8
|
1.0
|
CE1
|
A:HIS290
|
3.0
|
28.2
|
1.0
|
CG
|
A:HIS240
|
3.0
|
25.3
|
1.0
|
CE1
|
A:HIS240
|
3.0
|
25.0
|
1.0
|
N1
|
A:AZI607
|
3.0
|
37.1
|
1.0
|
CD2
|
A:HIS290
|
3.1
|
26.9
|
1.0
|
N2
|
A:AZI607
|
3.3
|
35.0
|
1.0
|
CB
|
A:HIS240
|
3.3
|
24.8
|
1.0
|
N3
|
A:AZI606
|
3.8
|
36.9
|
1.0
|
CA
|
A:HIS240
|
3.8
|
23.4
|
1.0
|
N3
|
A:AZI607
|
4.0
|
37.3
|
1.0
|
ND1
|
A:HIS291
|
4.1
|
26.1
|
1.0
|
CG
|
A:HIS291
|
4.1
|
24.7
|
1.0
|
ND1
|
A:HIS290
|
4.1
|
27.9
|
1.0
|
CD2
|
A:HIS240
|
4.2
|
24.4
|
1.0
|
NE2
|
A:HIS240
|
4.2
|
24.4
|
1.0
|
CG
|
A:HIS290
|
4.2
|
28.6
|
1.0
|
ND
|
A:HEA602
|
4.6
|
23.7
|
0.5
|
C1A
|
A:HEA602
|
4.6
|
28.1
|
0.5
|
C4D
|
A:HEA602
|
4.6
|
22.6
|
0.5
|
C1A
|
A:HEA602
|
4.7
|
26.5
|
0.5
|
CHA
|
A:HEA602
|
4.7
|
23.0
|
0.5
|
NA
|
A:HEA602
|
4.7
|
27.2
|
0.5
|
N
|
A:HIS240
|
4.7
|
23.6
|
1.0
|
CG2
|
A:VAL243
|
4.8
|
25.3
|
1.0
|
NA
|
A:HEA602
|
4.9
|
26.9
|
0.5
|
CHA
|
A:HEA602
|
4.9
|
28.6
|
0.5
|
FE
|
A:HEA602
|
4.9
|
26.0
|
0.5
|
FE
|
A:HEA602
|
4.9
|
28.9
|
0.5
|
C
|
A:HIS240
|
4.9
|
24.7
|
1.0
|
|
Copper binding site 2 out
of 6 in 5z84
Go back to
Copper Binding Sites List in 5z84
Copper binding site 2 out
of 6 in the The Structure of Azide-Bound Cytochrome C Oxidase Determined Using the Crystals Exposed to 20 Mm Azide Solution For 4 Days
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of The Structure of Azide-Bound Cytochrome C Oxidase Determined Using the Crystals Exposed to 20 Mm Azide Solution For 4 Days within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu302
b:31.4
occ:1.00
|
CU1
|
B:CUA302
|
0.0
|
31.4
|
1.0
|
ND1
|
B:HIS161
|
2.0
|
28.5
|
1.0
|
SG
|
B:CYS196
|
2.3
|
29.6
|
1.0
|
SG
|
B:CYS200
|
2.3
|
29.3
|
1.0
|
SD
|
B:MET207
|
2.4
|
31.5
|
1.0
|
CU2
|
B:CUA302
|
2.5
|
30.6
|
1.0
|
CE1
|
B:HIS161
|
3.0
|
28.5
|
1.0
|
CE
|
B:MET207
|
3.1
|
29.6
|
1.0
|
CG
|
B:HIS161
|
3.2
|
29.8
|
1.0
|
CB
|
B:CYS200
|
3.3
|
27.3
|
1.0
|
CB
|
B:CYS196
|
3.4
|
26.9
|
1.0
|
CG
|
B:MET207
|
3.5
|
31.8
|
1.0
|
CB
|
B:HIS161
|
3.6
|
25.4
|
1.0
|
O
|
B:GLU198
|
4.0
|
30.5
|
1.0
|
NE2
|
B:HIS161
|
4.2
|
29.6
|
1.0
|
CA
|
B:HIS161
|
4.2
|
28.4
|
1.0
|
CD2
|
B:HIS161
|
4.3
|
28.2
|
1.0
|
ND1
|
B:HIS204
|
4.4
|
31.9
|
1.0
|
CA
|
B:HIS204
|
4.7
|
29.9
|
1.0
|
CD1
|
B:TRP104
|
4.7
|
30.9
|
1.0
|
O
|
B:HIS102
|
4.7
|
30.4
|
1.0
|
O
|
B:LEU160
|
4.7
|
29.4
|
1.0
|
CA
|
B:CYS200
|
4.8
|
28.3
|
1.0
|
CA
|
B:CYS196
|
4.8
|
28.6
|
1.0
|
CB
|
B:MET207
|
4.8
|
30.9
|
1.0
|
O
|
B:HIS204
|
4.9
|
33.1
|
1.0
|
|
Copper binding site 3 out
of 6 in 5z84
Go back to
Copper Binding Sites List in 5z84
Copper binding site 3 out
of 6 in the The Structure of Azide-Bound Cytochrome C Oxidase Determined Using the Crystals Exposed to 20 Mm Azide Solution For 4 Days
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of The Structure of Azide-Bound Cytochrome C Oxidase Determined Using the Crystals Exposed to 20 Mm Azide Solution For 4 Days within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu302
b:30.6
occ:1.00
|
CU2
|
B:CUA302
|
0.0
|
30.6
|
1.0
|
ND1
|
B:HIS204
|
2.0
|
31.9
|
1.0
|
SG
|
B:CYS200
|
2.3
|
29.3
|
1.0
|
SG
|
B:CYS196
|
2.3
|
29.6
|
1.0
|
O
|
B:GLU198
|
2.4
|
30.5
|
1.0
|
CU1
|
B:CUA302
|
2.5
|
31.4
|
1.0
|
CE1
|
B:HIS204
|
2.9
|
32.8
|
1.0
|
CG
|
B:HIS204
|
3.1
|
31.4
|
1.0
|
CB
|
B:CYS196
|
3.3
|
26.9
|
1.0
|
CB
|
B:CYS200
|
3.3
|
27.3
|
1.0
|
C
|
B:GLU198
|
3.5
|
26.8
|
1.0
|
CB
|
B:HIS204
|
3.5
|
28.7
|
1.0
|
CA
|
B:HIS204
|
3.6
|
29.9
|
1.0
|
N
|
B:CYS200
|
3.7
|
28.0
|
1.0
|
O
|
B:HIS204
|
3.8
|
33.1
|
1.0
|
NE2
|
B:HIS204
|
4.0
|
31.1
|
1.0
|
N
|
B:GLU198
|
4.1
|
26.9
|
1.0
|
CD2
|
B:HIS204
|
4.1
|
30.2
|
1.0
|
ND1
|
B:HIS161
|
4.1
|
28.5
|
1.0
|
C
|
B:ILE199
|
4.1
|
27.5
|
1.0
|
C
|
B:HIS204
|
4.2
|
30.6
|
1.0
|
CA
|
B:CYS200
|
4.2
|
28.3
|
1.0
|
CA
|
B:ILE199
|
4.2
|
29.6
|
1.0
|
C
|
B:CYS196
|
4.3
|
30.3
|
1.0
|
N
|
B:ILE199
|
4.3
|
28.2
|
1.0
|
O
|
B:CYS196
|
4.3
|
28.1
|
1.0
|
SD
|
B:MET207
|
4.3
|
31.5
|
1.0
|
CA
|
B:CYS196
|
4.4
|
28.6
|
1.0
|
CA
|
B:GLU198
|
4.5
|
28.9
|
1.0
|
CG
|
B:MET207
|
4.6
|
31.8
|
1.0
|
N
|
B:SER197
|
4.6
|
30.0
|
1.0
|
CA
|
B:HIS161
|
4.9
|
28.4
|
1.0
|
N
|
B:HIS204
|
4.9
|
31.8
|
1.0
|
CG
|
B:HIS161
|
5.0
|
29.8
|
1.0
|
|
Copper binding site 4 out
of 6 in 5z84
Go back to
Copper Binding Sites List in 5z84
Copper binding site 4 out
of 6 in the The Structure of Azide-Bound Cytochrome C Oxidase Determined Using the Crystals Exposed to 20 Mm Azide Solution For 4 Days
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of The Structure of Azide-Bound Cytochrome C Oxidase Determined Using the Crystals Exposed to 20 Mm Azide Solution For 4 Days within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
N:Cu604
b:33.5
occ:1.00
|
N1
|
N:AZI607
|
1.8
|
40.1
|
1.0
|
ND1
|
N:HIS240
|
2.0
|
29.9
|
1.0
|
NE2
|
N:HIS291
|
2.0
|
32.7
|
1.0
|
NE2
|
N:HIS290
|
2.0
|
31.1
|
1.0
|
N2
|
N:AZI607
|
2.7
|
42.2
|
1.0
|
CE1
|
N:HIS291
|
2.9
|
27.9
|
1.0
|
CD2
|
N:HIS291
|
3.0
|
31.0
|
1.0
|
CE1
|
N:HIS240
|
3.0
|
27.7
|
1.0
|
CG
|
N:HIS240
|
3.0
|
31.6
|
1.0
|
CE1
|
N:HIS290
|
3.0
|
29.7
|
1.0
|
N1
|
N:AZI608
|
3.0
|
41.9
|
1.0
|
CD2
|
N:HIS290
|
3.1
|
28.9
|
1.0
|
CB
|
N:HIS240
|
3.3
|
28.2
|
1.0
|
N2
|
N:AZI608
|
3.3
|
39.9
|
1.0
|
CA
|
N:HIS240
|
3.8
|
29.6
|
1.0
|
N3
|
N:AZI607
|
3.9
|
39.3
|
1.0
|
N3
|
N:AZI608
|
4.0
|
39.4
|
1.0
|
ND1
|
N:HIS291
|
4.1
|
30.6
|
1.0
|
CG
|
N:HIS291
|
4.1
|
30.9
|
1.0
|
CD2
|
N:HIS240
|
4.1
|
28.9
|
1.0
|
NE2
|
N:HIS240
|
4.1
|
26.8
|
1.0
|
ND1
|
N:HIS290
|
4.2
|
29.6
|
1.0
|
CG
|
N:HIS290
|
4.2
|
31.6
|
1.0
|
C1A
|
N:HEA603
|
4.6
|
27.4
|
0.5
|
ND
|
N:HEA603
|
4.6
|
32.9
|
0.5
|
C4D
|
N:HEA603
|
4.6
|
32.4
|
0.5
|
NA
|
N:HEA603
|
4.6
|
29.4
|
0.5
|
N
|
N:HIS240
|
4.7
|
26.4
|
1.0
|
CHA
|
N:HEA603
|
4.8
|
30.0
|
0.5
|
CG2
|
N:VAL243
|
4.8
|
29.1
|
1.0
|
C1A
|
N:HEA603
|
4.8
|
35.0
|
0.5
|
CHA
|
N:HEA603
|
4.8
|
27.6
|
0.5
|
FE
|
N:HEA603
|
4.9
|
28.1
|
0.5
|
FE
|
N:HEA603
|
4.9
|
34.4
|
0.5
|
C
|
N:HIS240
|
4.9
|
26.9
|
1.0
|
NA
|
N:HEA603
|
5.0
|
36.1
|
0.5
|
C2A
|
N:HEA603
|
5.0
|
29.4
|
0.5
|
C4D
|
N:HEA603
|
5.0
|
29.3
|
0.5
|
C4A
|
N:HEA603
|
5.0
|
29.2
|
0.5
|
ND
|
N:HEA603
|
5.0
|
29.4
|
0.5
|
|
Copper binding site 5 out
of 6 in 5z84
Go back to
Copper Binding Sites List in 5z84
Copper binding site 5 out
of 6 in the The Structure of Azide-Bound Cytochrome C Oxidase Determined Using the Crystals Exposed to 20 Mm Azide Solution For 4 Days
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of The Structure of Azide-Bound Cytochrome C Oxidase Determined Using the Crystals Exposed to 20 Mm Azide Solution For 4 Days within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
O:Cu301
b:36.6
occ:1.00
|
CU1
|
O:CUA301
|
0.0
|
36.6
|
1.0
|
ND1
|
O:HIS161
|
2.1
|
38.5
|
1.0
|
SG
|
O:CYS200
|
2.3
|
34.2
|
1.0
|
SG
|
O:CYS196
|
2.3
|
37.0
|
1.0
|
SD
|
O:MET207
|
2.4
|
37.9
|
1.0
|
CU2
|
O:CUA301
|
2.5
|
36.2
|
1.0
|
CE1
|
O:HIS161
|
2.9
|
33.4
|
1.0
|
CE
|
O:MET207
|
3.1
|
35.8
|
1.0
|
CG
|
O:HIS161
|
3.2
|
34.1
|
1.0
|
CB
|
O:CYS200
|
3.2
|
32.5
|
1.0
|
CB
|
O:CYS196
|
3.4
|
35.2
|
1.0
|
CG
|
O:MET207
|
3.6
|
38.6
|
1.0
|
CB
|
O:HIS161
|
3.6
|
32.8
|
1.0
|
O
|
O:GLU198
|
3.9
|
33.4
|
1.0
|
NE2
|
O:HIS161
|
4.1
|
35.5
|
1.0
|
CA
|
O:HIS161
|
4.2
|
32.4
|
1.0
|
CD2
|
O:HIS161
|
4.3
|
35.2
|
1.0
|
ND1
|
O:HIS204
|
4.4
|
36.4
|
1.0
|
CD1
|
O:TRP104
|
4.7
|
40.2
|
1.0
|
O
|
O:LEU160
|
4.7
|
36.3
|
1.0
|
CA
|
O:HIS204
|
4.7
|
36.8
|
1.0
|
CA
|
O:CYS200
|
4.7
|
37.0
|
1.0
|
O
|
O:HIS102
|
4.7
|
36.8
|
1.0
|
CA
|
O:CYS196
|
4.8
|
35.2
|
1.0
|
CB
|
O:MET207
|
4.9
|
38.5
|
1.0
|
O
|
O:HIS204
|
5.0
|
38.8
|
1.0
|
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Copper binding site 6 out
of 6 in 5z84
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Copper Binding Sites List in 5z84
Copper binding site 6 out
of 6 in the The Structure of Azide-Bound Cytochrome C Oxidase Determined Using the Crystals Exposed to 20 Mm Azide Solution For 4 Days
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Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of The Structure of Azide-Bound Cytochrome C Oxidase Determined Using the Crystals Exposed to 20 Mm Azide Solution For 4 Days within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
O:Cu301
b:36.2
occ:1.00
|
CU2
|
O:CUA301
|
0.0
|
36.2
|
1.0
|
ND1
|
O:HIS204
|
2.0
|
36.4
|
1.0
|
O
|
O:GLU198
|
2.3
|
33.4
|
1.0
|
SG
|
O:CYS200
|
2.3
|
34.2
|
1.0
|
SG
|
O:CYS196
|
2.3
|
37.0
|
1.0
|
CU1
|
O:CUA301
|
2.5
|
36.6
|
1.0
|
CE1
|
O:HIS204
|
2.8
|
37.1
|
1.0
|
CG
|
O:HIS204
|
3.1
|
34.8
|
1.0
|
CB
|
O:CYS196
|
3.2
|
35.2
|
1.0
|
CB
|
O:CYS200
|
3.3
|
32.5
|
1.0
|
C
|
O:GLU198
|
3.4
|
32.1
|
1.0
|
CA
|
O:HIS204
|
3.6
|
36.8
|
1.0
|
CB
|
O:HIS204
|
3.6
|
36.3
|
1.0
|
N
|
O:CYS200
|
3.7
|
37.3
|
1.0
|
O
|
O:HIS204
|
3.9
|
38.8
|
1.0
|
NE2
|
O:HIS204
|
4.0
|
35.6
|
1.0
|
N
|
O:GLU198
|
4.1
|
33.1
|
1.0
|
C
|
O:ILE199
|
4.2
|
36.8
|
1.0
|
CD2
|
O:HIS204
|
4.2
|
32.7
|
1.0
|
C
|
O:HIS204
|
4.2
|
34.9
|
1.0
|
CA
|
O:CYS200
|
4.2
|
37.0
|
1.0
|
ND1
|
O:HIS161
|
4.2
|
38.5
|
1.0
|
CA
|
O:ILE199
|
4.2
|
37.6
|
1.0
|
C
|
O:CYS196
|
4.2
|
38.3
|
1.0
|
N
|
O:ILE199
|
4.2
|
33.8
|
1.0
|
O
|
O:CYS196
|
4.2
|
36.9
|
1.0
|
SD
|
O:MET207
|
4.4
|
37.9
|
1.0
|
CA
|
O:CYS196
|
4.4
|
35.2
|
1.0
|
CA
|
O:GLU198
|
4.4
|
33.9
|
1.0
|
N
|
O:SER197
|
4.6
|
37.2
|
1.0
|
CG
|
O:MET207
|
4.7
|
38.6
|
1.0
|
CA
|
O:HIS161
|
4.9
|
32.4
|
1.0
|
N
|
O:HIS204
|
4.9
|
36.0
|
1.0
|
|
Reference:
A.Shimada,
K.Hatano,
H.Tadehara,
N.Yano,
K.Shinzawa-Itoh,
E.Yamashita,
K.Muramoto,
T.Tsukihara,
S.Yoshikawa.
X-Ray Structural Analyses of Azide-Bound Cytochromecoxidases Reveal That the H-Pathway Is Critically Important For the Proton-Pumping Activity. J. Biol. Chem. V. 293 14868 2018.
ISSN: ESSN 1083-351X
PubMed: 30077971
DOI: 10.1074/JBC.RA118.003123
Page generated: Wed Jul 31 05:34:30 2024
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