Iron in PDB 3om3: Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State
Enzymatic activity of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State
All present enzymatic activity of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State:
1.9.3.1;
Protein crystallography data
The structure of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State, PDB code: 3om3
was solved by
J.Liu,
L.Qin,
S.Ferguson-Miller,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
40.46 /
2.60
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
124.650,
132.365,
178.006,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19.8 /
22.9
|
Other elements in 3om3:
The structure of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State
(pdb code 3om3). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the
Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State, PDB code: 3om3:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 3om3
Go back to
Iron Binding Sites List in 3om3
Iron binding site 1 out
of 4 in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe1
b:32.9
occ:1.00
|
FE
|
A:HEA1
|
0.0
|
32.9
|
1.0
|
NE2
|
A:HIS102
|
2.0
|
31.3
|
1.0
|
NB
|
A:HEA1
|
2.0
|
35.2
|
1.0
|
NC
|
A:HEA1
|
2.1
|
36.5
|
1.0
|
ND
|
A:HEA1
|
2.1
|
36.1
|
1.0
|
NA
|
A:HEA1
|
2.1
|
34.7
|
1.0
|
NE2
|
A:HIS421
|
2.2
|
36.7
|
1.0
|
CE1
|
A:HIS102
|
2.9
|
31.8
|
1.0
|
C4B
|
A:HEA1
|
3.0
|
35.9
|
1.0
|
CD2
|
A:HIS102
|
3.0
|
33.3
|
1.0
|
C1B
|
A:HEA1
|
3.0
|
34.3
|
1.0
|
CE1
|
A:HIS421
|
3.0
|
39.1
|
1.0
|
C1C
|
A:HEA1
|
3.1
|
36.3
|
1.0
|
C4D
|
A:HEA1
|
3.1
|
36.3
|
1.0
|
C4A
|
A:HEA1
|
3.1
|
34.8
|
1.0
|
C1D
|
A:HEA1
|
3.1
|
36.9
|
1.0
|
C1A
|
A:HEA1
|
3.1
|
34.4
|
1.0
|
C4C
|
A:HEA1
|
3.1
|
36.4
|
1.0
|
CD2
|
A:HIS421
|
3.2
|
37.6
|
1.0
|
CHC
|
A:HEA1
|
3.4
|
35.2
|
1.0
|
CHB
|
A:HEA1
|
3.4
|
35.4
|
1.0
|
CHA
|
A:HEA1
|
3.5
|
35.5
|
1.0
|
CHD
|
A:HEA1
|
3.5
|
35.6
|
1.0
|
ND1
|
A:HIS102
|
4.0
|
33.0
|
1.0
|
CG
|
A:HIS102
|
4.1
|
33.2
|
1.0
|
ND1
|
A:HIS421
|
4.2
|
39.5
|
1.0
|
C3B
|
A:HEA1
|
4.2
|
36.0
|
1.0
|
C2B
|
A:HEA1
|
4.2
|
35.1
|
1.0
|
C2C
|
A:HEA1
|
4.3
|
37.2
|
1.0
|
CG
|
A:HIS421
|
4.3
|
38.4
|
1.0
|
C3D
|
A:HEA1
|
4.3
|
36.3
|
1.0
|
C3A
|
A:HEA1
|
4.3
|
34.2
|
1.0
|
C2A
|
A:HEA1
|
4.3
|
34.5
|
1.0
|
C2D
|
A:HEA1
|
4.3
|
36.5
|
1.0
|
C3C
|
A:HEA1
|
4.3
|
36.3
|
1.0
|
CG2
|
A:THR48
|
4.5
|
35.3
|
1.0
|
|
Iron binding site 2 out
of 4 in 3om3
Go back to
Iron Binding Sites List in 3om3
Iron binding site 2 out
of 4 in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe2
b:46.7
occ:1.00
|
FE
|
A:HEA2
|
0.0
|
46.7
|
1.0
|
ND
|
A:HEA2
|
2.1
|
44.0
|
1.0
|
NE2
|
A:HIS419
|
2.1
|
37.1
|
1.0
|
NA
|
A:HEA2
|
2.1
|
47.7
|
1.0
|
NC
|
A:HEA2
|
2.1
|
47.6
|
1.0
|
NB
|
A:HEA2
|
2.2
|
50.4
|
1.0
|
C4D
|
A:HEA2
|
3.0
|
45.3
|
1.0
|
CE1
|
A:HIS419
|
3.1
|
37.6
|
1.0
|
C1D
|
A:HEA2
|
3.1
|
45.1
|
1.0
|
CD2
|
A:HIS419
|
3.1
|
37.3
|
1.0
|
C1A
|
A:HEA2
|
3.1
|
47.2
|
1.0
|
C1C
|
A:HEA2
|
3.1
|
48.0
|
1.0
|
C4C
|
A:HEA2
|
3.2
|
47.7
|
1.0
|
C4A
|
A:HEA2
|
3.2
|
48.8
|
1.0
|
C4B
|
A:HEA2
|
3.2
|
50.4
|
1.0
|
C1B
|
A:HEA2
|
3.2
|
51.1
|
1.0
|
CHA
|
A:HEA2
|
3.4
|
46.4
|
1.0
|
CHD
|
A:HEA2
|
3.5
|
46.7
|
1.0
|
CHC
|
A:HEA2
|
3.5
|
49.3
|
1.0
|
CHB
|
A:HEA2
|
3.5
|
49.1
|
1.0
|
ND1
|
A:HIS419
|
4.2
|
37.4
|
1.0
|
CG
|
A:HIS419
|
4.2
|
36.4
|
1.0
|
C3D
|
A:HEA2
|
4.3
|
44.4
|
1.0
|
C2D
|
A:HEA2
|
4.3
|
44.3
|
1.0
|
C2A
|
A:HEA2
|
4.4
|
48.0
|
1.0
|
C2C
|
A:HEA2
|
4.4
|
47.9
|
1.0
|
C3C
|
A:HEA2
|
4.4
|
47.6
|
1.0
|
C3A
|
A:HEA2
|
4.4
|
48.9
|
1.0
|
C2B
|
A:HEA2
|
4.4
|
51.7
|
1.0
|
C3B
|
A:HEA2
|
4.4
|
52.3
|
1.0
|
CG1
|
A:VAL423
|
4.7
|
42.8
|
1.0
|
CA
|
A:GLY398
|
4.9
|
48.9
|
1.0
|
|
Iron binding site 3 out
of 4 in 3om3
Go back to
Iron Binding Sites List in 3om3
Iron binding site 3 out
of 4 in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe1
b:47.9
occ:1.00
|
FE
|
C:HEA1
|
0.0
|
47.9
|
1.0
|
NB
|
C:HEA1
|
2.0
|
45.0
|
1.0
|
NE2
|
C:HIS102
|
2.0
|
52.7
|
1.0
|
ND
|
C:HEA1
|
2.0
|
45.5
|
1.0
|
NC
|
C:HEA1
|
2.1
|
46.7
|
1.0
|
NE2
|
C:HIS421
|
2.1
|
47.9
|
1.0
|
NA
|
C:HEA1
|
2.2
|
46.8
|
1.0
|
C4B
|
C:HEA1
|
3.0
|
47.2
|
1.0
|
CE1
|
C:HIS102
|
3.0
|
52.3
|
1.0
|
CD2
|
C:HIS102
|
3.0
|
53.1
|
1.0
|
CE1
|
C:HIS421
|
3.0
|
48.7
|
1.0
|
C1D
|
C:HEA1
|
3.0
|
46.4
|
1.0
|
C1B
|
C:HEA1
|
3.1
|
46.3
|
1.0
|
C1C
|
C:HEA1
|
3.1
|
47.0
|
1.0
|
C4C
|
C:HEA1
|
3.1
|
45.9
|
1.0
|
C4D
|
C:HEA1
|
3.1
|
46.0
|
1.0
|
C4A
|
C:HEA1
|
3.2
|
46.2
|
1.0
|
C1A
|
C:HEA1
|
3.2
|
45.9
|
1.0
|
CD2
|
C:HIS421
|
3.2
|
48.6
|
1.0
|
CHC
|
C:HEA1
|
3.4
|
46.6
|
1.0
|
CHD
|
C:HEA1
|
3.4
|
46.4
|
1.0
|
CHB
|
C:HEA1
|
3.5
|
46.5
|
1.0
|
CHA
|
C:HEA1
|
3.5
|
46.0
|
1.0
|
ND1
|
C:HIS102
|
4.1
|
52.7
|
1.0
|
CG
|
C:HIS102
|
4.2
|
53.0
|
1.0
|
ND1
|
C:HIS421
|
4.2
|
49.9
|
1.0
|
C3B
|
C:HEA1
|
4.2
|
48.5
|
1.0
|
C2B
|
C:HEA1
|
4.3
|
47.5
|
1.0
|
C2D
|
C:HEA1
|
4.3
|
46.5
|
1.0
|
C3D
|
C:HEA1
|
4.3
|
46.3
|
1.0
|
CG
|
C:HIS421
|
4.3
|
48.9
|
1.0
|
C3C
|
C:HEA1
|
4.3
|
46.2
|
1.0
|
C2C
|
C:HEA1
|
4.3
|
47.5
|
1.0
|
C3A
|
C:HEA1
|
4.4
|
46.1
|
1.0
|
C2A
|
C:HEA1
|
4.4
|
46.3
|
1.0
|
CG2
|
C:THR48
|
4.7
|
56.1
|
1.0
|
|
Iron binding site 4 out
of 4 in 3om3
Go back to
Iron Binding Sites List in 3om3
Iron binding site 4 out
of 4 in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe2
b:49.7
occ:1.00
|
FE
|
C:HEA2
|
0.0
|
49.7
|
1.0
|
ND
|
C:HEA2
|
2.0
|
52.1
|
1.0
|
NA
|
C:HEA2
|
2.1
|
51.3
|
1.0
|
NE2
|
C:HIS419
|
2.1
|
46.5
|
1.0
|
NC
|
C:HEA2
|
2.2
|
54.6
|
1.0
|
NB
|
C:HEA2
|
2.2
|
53.6
|
1.0
|
C4D
|
C:HEA2
|
3.0
|
51.9
|
1.0
|
C1D
|
C:HEA2
|
3.0
|
52.6
|
1.0
|
C1A
|
C:HEA2
|
3.0
|
49.9
|
1.0
|
CE1
|
C:HIS419
|
3.1
|
47.2
|
1.0
|
C4A
|
C:HEA2
|
3.1
|
52.1
|
1.0
|
C4C
|
C:HEA2
|
3.1
|
53.8
|
1.0
|
CD2
|
C:HIS419
|
3.2
|
47.0
|
1.0
|
C1B
|
C:HEA2
|
3.2
|
54.1
|
1.0
|
C1C
|
C:HEA2
|
3.2
|
54.0
|
1.0
|
C4B
|
C:HEA2
|
3.2
|
54.4
|
1.0
|
CHA
|
C:HEA2
|
3.3
|
51.5
|
1.0
|
CHD
|
C:HEA2
|
3.4
|
53.1
|
1.0
|
CHB
|
C:HEA2
|
3.5
|
52.9
|
1.0
|
CHC
|
C:HEA2
|
3.6
|
53.9
|
1.0
|
C3D
|
C:HEA2
|
4.2
|
51.5
|
1.0
|
ND1
|
C:HIS419
|
4.2
|
46.9
|
1.0
|
C2D
|
C:HEA2
|
4.2
|
52.5
|
1.0
|
CG
|
C:HIS419
|
4.3
|
47.4
|
1.0
|
C2A
|
C:HEA2
|
4.3
|
50.5
|
1.0
|
C3A
|
C:HEA2
|
4.3
|
51.0
|
1.0
|
C3C
|
C:HEA2
|
4.4
|
54.1
|
1.0
|
C2C
|
C:HEA2
|
4.4
|
54.3
|
1.0
|
C2B
|
C:HEA2
|
4.4
|
54.7
|
1.0
|
C3B
|
C:HEA2
|
4.5
|
55.3
|
1.0
|
CG1
|
C:VAL423
|
4.7
|
53.1
|
1.0
|
CA
|
C:GLY398
|
4.9
|
52.2
|
1.0
|
|
Reference:
J.Liu,
L.Qin,
S.Ferguson-Miller.
Crystallographic and Online Spectral Evidence For Role of Conformational Change and Conserved Water in Cytochrome Oxidase Proton Pump. Proc.Natl.Acad.Sci.Usa V. 108 1284 2011.
ISSN: ISSN 0027-8424
PubMed: 21205904
DOI: 10.1073/PNAS.1012846108
Page generated: Sun Aug 4 17:11:58 2024
|