Iron in PDB 3wcu: The Structure of A Deoxygenated 400 kDa Hemoglobin Provides A More Accurate Description of the Cooperative Mechanism of Giant Hemoglobins: Deoxygenated Form
Protein crystallography data
The structure of The Structure of A Deoxygenated 400 kDa Hemoglobin Provides A More Accurate Description of the Cooperative Mechanism of Giant Hemoglobins: Deoxygenated Form, PDB code: 3wcu
was solved by
N.Numoto,
T.Nakagawa,
R.Ohara,
T.Hasegawa,
A.Kita,
T.Yoshida,
T.Maruyama,
K.Imai,
Y.Fukumori,
K.Miki,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
42.45 /
2.90
|
Space group
|
P 63
|
Cell size a, b, c (Å), α, β, γ (°)
|
108.872,
108.872,
195.157,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
24.6 /
29.2
|
Other elements in 3wcu:
The structure of The Structure of A Deoxygenated 400 kDa Hemoglobin Provides A More Accurate Description of the Cooperative Mechanism of Giant Hemoglobins: Deoxygenated Form also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the The Structure of A Deoxygenated 400 kDa Hemoglobin Provides A More Accurate Description of the Cooperative Mechanism of Giant Hemoglobins: Deoxygenated Form
(pdb code 3wcu). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the
The Structure of A Deoxygenated 400 kDa Hemoglobin Provides A More Accurate Description of the Cooperative Mechanism of Giant Hemoglobins: Deoxygenated Form, PDB code: 3wcu:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Iron binding site 1 out
of 8 in 3wcu
Go back to
Iron Binding Sites List in 3wcu
Iron binding site 1 out
of 8 in the The Structure of A Deoxygenated 400 kDa Hemoglobin Provides A More Accurate Description of the Cooperative Mechanism of Giant Hemoglobins: Deoxygenated Form
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 A Deoxygenated 400 kDa Hemoglobin Provides A More Accurate Description of the Cooperative Mechanism of Giant Hemoglobins: Deoxygenated Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe200
b:67.8
occ:1.00
|
FE
|
A:HEM200
|
0.0
|
67.8
|
1.0
|
NC
|
A:HEM200
|
2.0
|
67.8
|
1.0
|
NA
|
A:HEM200
|
2.0
|
67.8
|
1.0
|
ND
|
A:HEM200
|
2.0
|
67.8
|
1.0
|
NB
|
A:HEM200
|
2.0
|
67.8
|
1.0
|
NE2
|
A:HIS94
|
2.2
|
58.5
|
1.0
|
C4C
|
A:HEM200
|
3.0
|
67.8
|
1.0
|
C1D
|
A:HEM200
|
3.0
|
67.8
|
1.0
|
C1C
|
A:HEM200
|
3.0
|
67.8
|
1.0
|
C4D
|
A:HEM200
|
3.0
|
67.8
|
1.0
|
C1B
|
A:HEM200
|
3.0
|
67.8
|
1.0
|
C1A
|
A:HEM200
|
3.0
|
67.8
|
1.0
|
C4A
|
A:HEM200
|
3.1
|
67.8
|
1.0
|
CE1
|
A:HIS94
|
3.1
|
58.5
|
1.0
|
C4B
|
A:HEM200
|
3.1
|
67.8
|
1.0
|
CD2
|
A:HIS94
|
3.3
|
58.5
|
1.0
|
CHD
|
A:HEM200
|
3.4
|
67.8
|
1.0
|
CHB
|
A:HEM200
|
3.4
|
67.8
|
1.0
|
CHA
|
A:HEM200
|
3.4
|
67.8
|
1.0
|
CHC
|
A:HEM200
|
3.4
|
67.8
|
1.0
|
CG2
|
A:VAL66
|
4.0
|
37.5
|
1.0
|
ND1
|
A:HIS94
|
4.2
|
58.5
|
1.0
|
C3A
|
A:HEM200
|
4.3
|
67.8
|
1.0
|
C2A
|
A:HEM200
|
4.3
|
67.8
|
1.0
|
C2C
|
A:HEM200
|
4.3
|
67.8
|
1.0
|
C2B
|
A:HEM200
|
4.3
|
67.8
|
1.0
|
C3B
|
A:HEM200
|
4.3
|
67.8
|
1.0
|
C3D
|
A:HEM200
|
4.3
|
67.8
|
1.0
|
C3C
|
A:HEM200
|
4.3
|
67.8
|
1.0
|
C2D
|
A:HEM200
|
4.3
|
67.8
|
1.0
|
CG
|
A:HIS94
|
4.4
|
58.5
|
1.0
|
CG1
|
A:VAL66
|
4.6
|
37.5
|
1.0
|
CE1
|
A:HIS62
|
4.9
|
54.8
|
1.0
|
CB
|
A:VAL66
|
4.9
|
37.5
|
1.0
|
|
Iron binding site 2 out
of 8 in 3wcu
Go back to
Iron Binding Sites List in 3wcu
Iron binding site 2 out
of 8 in the The Structure of A Deoxygenated 400 kDa Hemoglobin Provides A More Accurate Description of the Cooperative Mechanism of Giant Hemoglobins: Deoxygenated Form
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 A Deoxygenated 400 kDa Hemoglobin Provides A More Accurate Description of the Cooperative Mechanism of Giant Hemoglobins: Deoxygenated Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe200
b:67.8
occ:1.00
|
FE
|
C:HEM200
|
0.0
|
67.8
|
1.0
|
ND
|
C:HEM200
|
2.0
|
67.8
|
1.0
|
NB
|
C:HEM200
|
2.0
|
67.8
|
1.0
|
NA
|
C:HEM200
|
2.0
|
67.8
|
1.0
|
NC
|
C:HEM200
|
2.0
|
67.8
|
1.0
|
NE2
|
C:HIS99
|
2.2
|
68.2
|
1.0
|
CE1
|
C:HIS99
|
2.9
|
68.2
|
1.0
|
C1D
|
C:HEM200
|
3.0
|
67.8
|
1.0
|
C4C
|
C:HEM200
|
3.0
|
67.8
|
1.0
|
C4D
|
C:HEM200
|
3.0
|
67.8
|
1.0
|
C1B
|
C:HEM200
|
3.0
|
67.8
|
1.0
|
C1C
|
C:HEM200
|
3.0
|
67.8
|
1.0
|
C4A
|
C:HEM200
|
3.1
|
67.8
|
1.0
|
C1A
|
C:HEM200
|
3.1
|
67.8
|
1.0
|
C4B
|
C:HEM200
|
3.1
|
67.8
|
1.0
|
CD2
|
C:HIS99
|
3.3
|
68.2
|
1.0
|
CHB
|
C:HEM200
|
3.4
|
67.8
|
1.0
|
CHD
|
C:HEM200
|
3.4
|
67.8
|
1.0
|
CHA
|
C:HEM200
|
3.4
|
67.8
|
1.0
|
CHC
|
C:HEM200
|
3.4
|
67.8
|
1.0
|
ND1
|
C:HIS99
|
4.1
|
68.2
|
1.0
|
CG2
|
C:VAL71
|
4.1
|
64.0
|
1.0
|
CG1
|
C:VAL71
|
4.3
|
64.0
|
1.0
|
C3A
|
C:HEM200
|
4.3
|
67.8
|
1.0
|
C3D
|
C:HEM200
|
4.3
|
67.8
|
1.0
|
C2B
|
C:HEM200
|
4.3
|
67.8
|
1.0
|
C2D
|
C:HEM200
|
4.3
|
67.8
|
1.0
|
C3B
|
C:HEM200
|
4.3
|
67.8
|
1.0
|
C2A
|
C:HEM200
|
4.3
|
67.8
|
1.0
|
C2C
|
C:HEM200
|
4.3
|
67.8
|
1.0
|
CG
|
C:HIS99
|
4.3
|
68.2
|
1.0
|
C3C
|
C:HEM200
|
4.3
|
67.8
|
1.0
|
CB
|
C:VAL71
|
4.8
|
64.0
|
1.0
|
|
Iron binding site 3 out
of 8 in 3wcu
Go back to
Iron Binding Sites List in 3wcu
Iron binding site 3 out
of 8 in the The Structure of A Deoxygenated 400 kDa Hemoglobin Provides A More Accurate Description of the Cooperative Mechanism of Giant Hemoglobins: Deoxygenated Form
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 A Deoxygenated 400 kDa Hemoglobin Provides A More Accurate Description of the Cooperative Mechanism of Giant Hemoglobins: Deoxygenated Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe201
b:67.8
occ:1.00
|
FE
|
B:HEM201
|
0.0
|
67.8
|
1.0
|
NC
|
B:HEM201
|
2.0
|
67.8
|
1.0
|
NB
|
B:HEM201
|
2.0
|
67.8
|
1.0
|
NA
|
B:HEM201
|
2.0
|
67.8
|
1.0
|
ND
|
B:HEM201
|
2.0
|
67.8
|
1.0
|
NE2
|
B:HIS95
|
2.1
|
91.6
|
1.0
|
C1D
|
B:HEM201
|
3.0
|
67.8
|
1.0
|
C4C
|
B:HEM201
|
3.0
|
67.8
|
1.0
|
CD2
|
B:HIS95
|
3.0
|
91.6
|
1.0
|
C4D
|
B:HEM201
|
3.0
|
67.8
|
1.0
|
C1B
|
B:HEM201
|
3.0
|
67.8
|
1.0
|
C1C
|
B:HEM201
|
3.0
|
67.8
|
1.0
|
C4A
|
B:HEM201
|
3.1
|
67.8
|
1.0
|
C1A
|
B:HEM201
|
3.1
|
67.8
|
1.0
|
C4B
|
B:HEM201
|
3.1
|
67.8
|
1.0
|
CE1
|
B:HIS95
|
3.2
|
91.6
|
1.0
|
CHD
|
B:HEM201
|
3.4
|
67.8
|
1.0
|
CHB
|
B:HEM201
|
3.4
|
67.8
|
1.0
|
CHA
|
B:HEM201
|
3.4
|
67.8
|
1.0
|
CHC
|
B:HEM201
|
3.4
|
67.8
|
1.0
|
CG
|
B:HIS95
|
4.2
|
91.6
|
1.0
|
ND1
|
B:HIS95
|
4.2
|
91.6
|
1.0
|
C3D
|
B:HEM201
|
4.3
|
67.8
|
1.0
|
C2A
|
B:HEM201
|
4.3
|
67.8
|
1.0
|
C3A
|
B:HEM201
|
4.3
|
67.8
|
1.0
|
C2B
|
B:HEM201
|
4.3
|
67.8
|
1.0
|
C2C
|
B:HEM201
|
4.3
|
67.8
|
1.0
|
C3B
|
B:HEM201
|
4.3
|
67.8
|
1.0
|
C2D
|
B:HEM201
|
4.3
|
67.8
|
1.0
|
C3C
|
B:HEM201
|
4.3
|
67.8
|
1.0
|
CG2
|
B:VAL67
|
4.4
|
52.9
|
1.0
|
CG1
|
B:VAL67
|
4.9
|
52.9
|
1.0
|
|
Iron binding site 4 out
of 8 in 3wcu
Go back to
Iron Binding Sites List in 3wcu
Iron binding site 4 out
of 8 in the The Structure of A Deoxygenated 400 kDa Hemoglobin Provides A More Accurate Description of the Cooperative Mechanism of Giant Hemoglobins: Deoxygenated Form
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 A Deoxygenated 400 kDa Hemoglobin Provides A More Accurate Description of the Cooperative Mechanism of Giant Hemoglobins: Deoxygenated Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe201
b:67.8
occ:1.00
|
FE
|
D:HEM201
|
0.0
|
67.8
|
1.0
|
NC
|
D:HEM201
|
2.0
|
67.8
|
1.0
|
NB
|
D:HEM201
|
2.0
|
67.8
|
1.0
|
NA
|
D:HEM201
|
2.0
|
67.8
|
1.0
|
ND
|
D:HEM201
|
2.0
|
67.8
|
1.0
|
NE2
|
D:HIS99
|
2.1
|
56.1
|
1.0
|
CD2
|
D:HIS99
|
3.0
|
56.1
|
1.0
|
C4C
|
D:HEM201
|
3.0
|
67.8
|
1.0
|
C1C
|
D:HEM201
|
3.0
|
67.8
|
1.0
|
C1D
|
D:HEM201
|
3.0
|
67.8
|
1.0
|
C1B
|
D:HEM201
|
3.0
|
67.8
|
1.0
|
C4D
|
D:HEM201
|
3.1
|
67.8
|
1.0
|
C4A
|
D:HEM201
|
3.1
|
67.8
|
1.0
|
C4B
|
D:HEM201
|
3.1
|
67.8
|
1.0
|
C1A
|
D:HEM201
|
3.1
|
67.8
|
1.0
|
CE1
|
D:HIS99
|
3.2
|
56.1
|
1.0
|
CHB
|
D:HEM201
|
3.4
|
67.8
|
1.0
|
CHD
|
D:HEM201
|
3.4
|
67.8
|
1.0
|
CHC
|
D:HEM201
|
3.4
|
67.8
|
1.0
|
CHA
|
D:HEM201
|
3.4
|
67.8
|
1.0
|
CG
|
D:HIS99
|
4.2
|
56.1
|
1.0
|
ND1
|
D:HIS99
|
4.2
|
56.1
|
1.0
|
C2C
|
D:HEM201
|
4.3
|
67.8
|
1.0
|
C3A
|
D:HEM201
|
4.3
|
67.8
|
1.0
|
C2A
|
D:HEM201
|
4.3
|
67.8
|
1.0
|
C3B
|
D:HEM201
|
4.3
|
67.8
|
1.0
|
C2B
|
D:HEM201
|
4.3
|
67.8
|
1.0
|
C3C
|
D:HEM201
|
4.3
|
67.8
|
1.0
|
C3D
|
D:HEM201
|
4.3
|
67.8
|
1.0
|
C2D
|
D:HEM201
|
4.3
|
67.8
|
1.0
|
CG2
|
D:VAL71
|
4.4
|
57.5
|
1.0
|
CG1
|
D:VAL71
|
4.6
|
57.5
|
1.0
|
CZ
|
D:PHE110
|
4.8
|
60.8
|
1.0
|
|
Iron binding site 5 out
of 8 in 3wcu
Go back to
Iron Binding Sites List in 3wcu
Iron binding site 5 out
of 8 in the The Structure of A Deoxygenated 400 kDa Hemoglobin Provides A More Accurate Description of the Cooperative Mechanism of Giant Hemoglobins: Deoxygenated Form
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 A Deoxygenated 400 kDa Hemoglobin Provides A More Accurate Description of the Cooperative Mechanism of Giant Hemoglobins: Deoxygenated Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Fe200
b:67.8
occ:1.00
|
FE
|
E:HEM200
|
0.0
|
67.8
|
1.0
|
NC
|
E:HEM200
|
2.0
|
67.8
|
1.0
|
NA
|
E:HEM200
|
2.0
|
67.8
|
1.0
|
ND
|
E:HEM200
|
2.0
|
67.8
|
1.0
|
NB
|
E:HEM200
|
2.0
|
67.8
|
1.0
|
NE2
|
E:HIS94
|
2.2
|
58.5
|
1.0
|
C4C
|
E:HEM200
|
3.0
|
67.8
|
1.0
|
C1D
|
E:HEM200
|
3.0
|
67.8
|
1.0
|
C1C
|
E:HEM200
|
3.0
|
67.8
|
1.0
|
C4D
|
E:HEM200
|
3.0
|
67.8
|
1.0
|
C1B
|
E:HEM200
|
3.0
|
67.8
|
1.0
|
C1A
|
E:HEM200
|
3.0
|
67.8
|
1.0
|
C4A
|
E:HEM200
|
3.1
|
67.8
|
1.0
|
CE1
|
E:HIS94
|
3.1
|
58.5
|
1.0
|
C4B
|
E:HEM200
|
3.1
|
67.8
|
1.0
|
CD2
|
E:HIS94
|
3.3
|
58.5
|
1.0
|
CHD
|
E:HEM200
|
3.4
|
67.8
|
1.0
|
CHB
|
E:HEM200
|
3.4
|
67.8
|
1.0
|
CHA
|
E:HEM200
|
3.4
|
67.8
|
1.0
|
CHC
|
E:HEM200
|
3.4
|
67.8
|
1.0
|
CG2
|
E:VAL66
|
4.0
|
37.5
|
1.0
|
ND1
|
E:HIS94
|
4.2
|
58.5
|
1.0
|
C3A
|
E:HEM200
|
4.3
|
67.8
|
1.0
|
C2A
|
E:HEM200
|
4.3
|
67.8
|
1.0
|
C2B
|
E:HEM200
|
4.3
|
67.8
|
1.0
|
C2C
|
E:HEM200
|
4.3
|
67.8
|
1.0
|
C3B
|
E:HEM200
|
4.3
|
67.8
|
1.0
|
C3D
|
E:HEM200
|
4.3
|
67.8
|
1.0
|
C3C
|
E:HEM200
|
4.3
|
67.8
|
1.0
|
C2D
|
E:HEM200
|
4.3
|
67.8
|
1.0
|
CG
|
E:HIS94
|
4.4
|
58.5
|
1.0
|
CG1
|
E:VAL66
|
4.6
|
37.5
|
1.0
|
CE1
|
E:HIS62
|
4.9
|
54.8
|
1.0
|
CB
|
E:VAL66
|
4.9
|
37.5
|
1.0
|
|
Iron binding site 6 out
of 8 in 3wcu
Go back to
Iron Binding Sites List in 3wcu
Iron binding site 6 out
of 8 in the The Structure of A Deoxygenated 400 kDa Hemoglobin Provides A More Accurate Description of the Cooperative Mechanism of Giant Hemoglobins: Deoxygenated Form
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 A Deoxygenated 400 kDa Hemoglobin Provides A More Accurate Description of the Cooperative Mechanism of Giant Hemoglobins: Deoxygenated Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Fe201
b:67.8
occ:1.00
|
FE
|
F:HEM201
|
0.0
|
67.8
|
1.0
|
NC
|
F:HEM201
|
2.0
|
67.8
|
1.0
|
NB
|
F:HEM201
|
2.0
|
67.8
|
1.0
|
ND
|
F:HEM201
|
2.0
|
67.8
|
1.0
|
NA
|
F:HEM201
|
2.0
|
67.8
|
1.0
|
NE2
|
F:HIS95
|
2.1
|
91.6
|
1.0
|
C1D
|
F:HEM201
|
3.0
|
67.8
|
1.0
|
C4C
|
F:HEM201
|
3.0
|
67.8
|
1.0
|
CD2
|
F:HIS95
|
3.0
|
91.6
|
1.0
|
C4D
|
F:HEM201
|
3.0
|
67.8
|
1.0
|
C1B
|
F:HEM201
|
3.0
|
67.8
|
1.0
|
C1C
|
F:HEM201
|
3.0
|
67.8
|
1.0
|
C4A
|
F:HEM201
|
3.1
|
67.8
|
1.0
|
C1A
|
F:HEM201
|
3.1
|
67.8
|
1.0
|
C4B
|
F:HEM201
|
3.1
|
67.8
|
1.0
|
CE1
|
F:HIS95
|
3.2
|
91.6
|
1.0
|
CHD
|
F:HEM201
|
3.4
|
67.8
|
1.0
|
CHB
|
F:HEM201
|
3.4
|
67.8
|
1.0
|
CHA
|
F:HEM201
|
3.4
|
67.8
|
1.0
|
CHC
|
F:HEM201
|
3.4
|
67.8
|
1.0
|
CG
|
F:HIS95
|
4.2
|
91.6
|
1.0
|
ND1
|
F:HIS95
|
4.2
|
91.6
|
1.0
|
C3D
|
F:HEM201
|
4.3
|
67.8
|
1.0
|
C2A
|
F:HEM201
|
4.3
|
67.8
|
1.0
|
C3A
|
F:HEM201
|
4.3
|
67.8
|
1.0
|
C2B
|
F:HEM201
|
4.3
|
67.8
|
1.0
|
C2C
|
F:HEM201
|
4.3
|
67.8
|
1.0
|
C3B
|
F:HEM201
|
4.3
|
67.8
|
1.0
|
C2D
|
F:HEM201
|
4.3
|
67.8
|
1.0
|
C3C
|
F:HEM201
|
4.3
|
67.8
|
1.0
|
CG2
|
F:VAL67
|
4.4
|
52.9
|
1.0
|
CG1
|
F:VAL67
|
4.9
|
52.9
|
1.0
|
|
Iron binding site 7 out
of 8 in 3wcu
Go back to
Iron Binding Sites List in 3wcu
Iron binding site 7 out
of 8 in the The Structure of A Deoxygenated 400 kDa Hemoglobin Provides A More Accurate Description of the Cooperative Mechanism of Giant Hemoglobins: Deoxygenated Form
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 A Deoxygenated 400 kDa Hemoglobin Provides A More Accurate Description of the Cooperative Mechanism of Giant Hemoglobins: Deoxygenated Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Fe200
b:67.8
occ:1.00
|
FE
|
G:HEM200
|
0.0
|
67.8
|
1.0
|
ND
|
G:HEM200
|
2.0
|
67.8
|
1.0
|
NB
|
G:HEM200
|
2.0
|
67.8
|
1.0
|
NA
|
G:HEM200
|
2.0
|
67.8
|
1.0
|
NC
|
G:HEM200
|
2.0
|
67.8
|
1.0
|
NE2
|
G:HIS99
|
2.2
|
68.2
|
1.0
|
CE1
|
G:HIS99
|
2.9
|
68.2
|
1.0
|
C1D
|
G:HEM200
|
3.0
|
67.8
|
1.0
|
C4C
|
G:HEM200
|
3.0
|
67.8
|
1.0
|
C1B
|
G:HEM200
|
3.0
|
67.8
|
1.0
|
C4D
|
G:HEM200
|
3.0
|
67.8
|
1.0
|
C1C
|
G:HEM200
|
3.0
|
67.8
|
1.0
|
C4A
|
G:HEM200
|
3.1
|
67.8
|
1.0
|
C1A
|
G:HEM200
|
3.1
|
67.8
|
1.0
|
C4B
|
G:HEM200
|
3.1
|
67.8
|
1.0
|
CD2
|
G:HIS99
|
3.3
|
68.2
|
1.0
|
CHB
|
G:HEM200
|
3.4
|
67.8
|
1.0
|
CHD
|
G:HEM200
|
3.4
|
67.8
|
1.0
|
CHA
|
G:HEM200
|
3.4
|
67.8
|
1.0
|
CHC
|
G:HEM200
|
3.4
|
67.8
|
1.0
|
ND1
|
G:HIS99
|
4.1
|
68.2
|
1.0
|
CG2
|
G:VAL71
|
4.1
|
64.0
|
1.0
|
CG1
|
G:VAL71
|
4.3
|
64.0
|
1.0
|
C3A
|
G:HEM200
|
4.3
|
67.8
|
1.0
|
C3D
|
G:HEM200
|
4.3
|
67.8
|
1.0
|
C2B
|
G:HEM200
|
4.3
|
67.8
|
1.0
|
C3B
|
G:HEM200
|
4.3
|
67.8
|
1.0
|
C2D
|
G:HEM200
|
4.3
|
67.8
|
1.0
|
C2A
|
G:HEM200
|
4.3
|
67.8
|
1.0
|
C2C
|
G:HEM200
|
4.3
|
67.8
|
1.0
|
CG
|
G:HIS99
|
4.3
|
68.2
|
1.0
|
C3C
|
G:HEM200
|
4.3
|
67.8
|
1.0
|
CB
|
G:VAL71
|
4.8
|
64.0
|
1.0
|
|
Iron binding site 8 out
of 8 in 3wcu
Go back to
Iron Binding Sites List in 3wcu
Iron binding site 8 out
of 8 in the The Structure of A Deoxygenated 400 kDa Hemoglobin Provides A More Accurate Description of the Cooperative Mechanism of Giant Hemoglobins: Deoxygenated Form
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 A Deoxygenated 400 kDa Hemoglobin Provides A More Accurate Description of the Cooperative Mechanism of Giant Hemoglobins: Deoxygenated Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Fe201
b:67.8
occ:1.00
|
FE
|
H:HEM201
|
0.0
|
67.8
|
1.0
|
NC
|
H:HEM201
|
2.0
|
67.8
|
1.0
|
NB
|
H:HEM201
|
2.0
|
67.8
|
1.0
|
NA
|
H:HEM201
|
2.0
|
67.8
|
1.0
|
ND
|
H:HEM201
|
2.0
|
67.8
|
1.0
|
NE2
|
H:HIS99
|
2.1
|
56.1
|
1.0
|
CD2
|
H:HIS99
|
3.0
|
56.1
|
1.0
|
C4C
|
H:HEM201
|
3.0
|
67.8
|
1.0
|
C1C
|
H:HEM201
|
3.0
|
67.8
|
1.0
|
C1D
|
H:HEM201
|
3.0
|
67.8
|
1.0
|
C1B
|
H:HEM201
|
3.0
|
67.8
|
1.0
|
C4D
|
H:HEM201
|
3.1
|
67.8
|
1.0
|
C4A
|
H:HEM201
|
3.1
|
67.8
|
1.0
|
C4B
|
H:HEM201
|
3.1
|
67.8
|
1.0
|
C1A
|
H:HEM201
|
3.1
|
67.8
|
1.0
|
CE1
|
H:HIS99
|
3.2
|
56.1
|
1.0
|
CHB
|
H:HEM201
|
3.4
|
67.8
|
1.0
|
CHD
|
H:HEM201
|
3.4
|
67.8
|
1.0
|
CHC
|
H:HEM201
|
3.4
|
67.8
|
1.0
|
CHA
|
H:HEM201
|
3.4
|
67.8
|
1.0
|
CG
|
H:HIS99
|
4.2
|
56.1
|
1.0
|
ND1
|
H:HIS99
|
4.2
|
56.1
|
1.0
|
C2C
|
H:HEM201
|
4.3
|
67.8
|
1.0
|
C3A
|
H:HEM201
|
4.3
|
67.8
|
1.0
|
C2A
|
H:HEM201
|
4.3
|
67.8
|
1.0
|
C3B
|
H:HEM201
|
4.3
|
67.8
|
1.0
|
C2B
|
H:HEM201
|
4.3
|
67.8
|
1.0
|
C3C
|
H:HEM201
|
4.3
|
67.8
|
1.0
|
C3D
|
H:HEM201
|
4.3
|
67.8
|
1.0
|
C2D
|
H:HEM201
|
4.3
|
67.8
|
1.0
|
CG2
|
H:VAL71
|
4.4
|
57.5
|
1.0
|
CG1
|
H:VAL71
|
4.6
|
57.5
|
1.0
|
CZ
|
H:PHE110
|
4.8
|
60.8
|
1.0
|
|
Reference:
N.Numoto,
T.Nakagawa,
R.Ohara,
T.Hasegawa,
A.Kita,
T.Yoshida,
T.Maruyama,
K.Imai,
Y.Fukumori,
K.Miki.
The Structure of A Deoxygenated 400 kDa Haemoglobin Reveals Ternary- and Quaternary-Structural Changes of Giant Haemoglobins Acta Crystallogr.,Sect.D V. 70 1823 2014.
ISSN: ISSN 0907-4449
PubMed: 25004960
DOI: 10.1107/S1399004714008475
Page generated: Sun Aug 4 22:35:18 2024
|