Iron in PDB 4n7o: Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin with Phosphate at 2.5 A Resolution.
Protein crystallography data
The structure of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin with Phosphate at 2.5 A Resolution., PDB code: 4n7o
was solved by
K.Sugiyama,
N.Shibayama,
S.Y.Park,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
20.00 /
2.50
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
228.935,
54.337,
137.884,
90.00,
103.22,
90.00
|
R / Rfree (%)
|
26.7 /
29.2
|
Other elements in 4n7o:
The structure of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin with Phosphate at 2.5 A Resolution. also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin with Phosphate at 2.5 A Resolution.
(pdb code 4n7o). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 6 binding sites of Iron where determined in the
Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin with Phosphate at 2.5 A Resolution., PDB code: 4n7o:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
Iron binding site 1 out
of 6 in 4n7o
Go back to
Iron Binding Sites List in 4n7o
Iron binding site 1 out
of 6 in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin with Phosphate at 2.5 A Resolution.
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin with Phosphate at 2.5 A Resolution. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe201
b:54.3
occ:1.00
|
FE
|
B:HEM201
|
0.0
|
54.3
|
1.0
|
NC
|
B:HEM201
|
2.0
|
54.2
|
1.0
|
NA
|
B:HEM201
|
2.1
|
58.1
|
1.0
|
NB
|
B:HEM201
|
2.1
|
56.0
|
1.0
|
ND
|
B:HEM201
|
2.1
|
56.1
|
1.0
|
NE2
|
B:HIS92
|
2.2
|
48.4
|
1.0
|
CD2
|
B:HIS92
|
3.0
|
48.8
|
1.0
|
C4C
|
B:HEM201
|
3.0
|
52.9
|
1.0
|
C4A
|
B:HEM201
|
3.1
|
59.8
|
1.0
|
C1B
|
B:HEM201
|
3.1
|
57.0
|
1.0
|
C1C
|
B:HEM201
|
3.1
|
52.8
|
1.0
|
C1D
|
B:HEM201
|
3.1
|
57.0
|
1.0
|
C1A
|
B:HEM201
|
3.1
|
59.9
|
1.0
|
C4D
|
B:HEM201
|
3.1
|
56.1
|
1.0
|
C4B
|
B:HEM201
|
3.2
|
54.3
|
1.0
|
CE1
|
B:HIS92
|
3.3
|
48.9
|
1.0
|
CHD
|
B:HEM201
|
3.4
|
55.0
|
1.0
|
CHB
|
B:HEM201
|
3.4
|
58.6
|
1.0
|
CHA
|
B:HEM201
|
3.5
|
58.2
|
1.0
|
CHC
|
B:HEM201
|
3.5
|
53.4
|
1.0
|
CG
|
B:HIS92
|
4.2
|
49.7
|
1.0
|
C3C
|
B:HEM201
|
4.3
|
51.1
|
1.0
|
C2C
|
B:HEM201
|
4.3
|
52.3
|
1.0
|
ND1
|
B:HIS92
|
4.3
|
49.1
|
1.0
|
C3A
|
B:HEM201
|
4.3
|
61.7
|
1.0
|
C2A
|
B:HEM201
|
4.4
|
63.2
|
1.0
|
C2B
|
B:HEM201
|
4.4
|
55.7
|
1.0
|
C2D
|
B:HEM201
|
4.4
|
56.5
|
1.0
|
C3B
|
B:HEM201
|
4.4
|
54.5
|
1.0
|
C3D
|
B:HEM201
|
4.4
|
56.8
|
1.0
|
NE2
|
B:HIS63
|
4.9
|
83.8
|
1.0
|
|
Iron binding site 2 out
of 6 in 4n7o
Go back to
Iron Binding Sites List in 4n7o
Iron binding site 2 out
of 6 in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin with Phosphate at 2.5 A Resolution.
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin with Phosphate at 2.5 A Resolution. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe201
b:59.4
occ:1.00
|
FE
|
C:HEM201
|
0.0
|
59.4
|
1.0
|
NC
|
C:HEM201
|
2.0
|
56.6
|
1.0
|
NB
|
C:HEM201
|
2.1
|
58.5
|
1.0
|
NA
|
C:HEM201
|
2.1
|
63.1
|
1.0
|
ND
|
C:HEM201
|
2.1
|
57.6
|
1.0
|
NE2
|
C:HIS87
|
2.5
|
86.4
|
1.0
|
C1B
|
C:HEM201
|
3.0
|
60.4
|
1.0
|
C4C
|
C:HEM201
|
3.0
|
54.6
|
1.0
|
CE1
|
C:HIS87
|
3.1
|
85.0
|
1.0
|
C1C
|
C:HEM201
|
3.1
|
55.5
|
1.0
|
C4A
|
C:HEM201
|
3.1
|
63.6
|
1.0
|
C1A
|
C:HEM201
|
3.1
|
64.2
|
1.0
|
C4B
|
C:HEM201
|
3.1
|
58.7
|
1.0
|
C1D
|
C:HEM201
|
3.1
|
55.0
|
1.0
|
C4D
|
C:HEM201
|
3.1
|
61.1
|
1.0
|
CHB
|
C:HEM201
|
3.4
|
63.3
|
1.0
|
CHD
|
C:HEM201
|
3.4
|
55.7
|
1.0
|
CHC
|
C:HEM201
|
3.5
|
57.1
|
1.0
|
CHA
|
C:HEM201
|
3.5
|
62.5
|
1.0
|
CD2
|
C:HIS87
|
3.6
|
86.2
|
1.0
|
NE2
|
C:HIS58
|
4.1
|
86.4
|
1.0
|
CE1
|
C:HIS58
|
4.1
|
84.9
|
1.0
|
ND1
|
C:HIS87
|
4.3
|
85.7
|
1.0
|
C3C
|
C:HEM201
|
4.3
|
53.8
|
1.0
|
C2C
|
C:HEM201
|
4.3
|
55.4
|
1.0
|
C2B
|
C:HEM201
|
4.3
|
60.0
|
1.0
|
C2A
|
C:HEM201
|
4.3
|
65.6
|
1.0
|
C3A
|
C:HEM201
|
4.3
|
64.9
|
1.0
|
C3B
|
C:HEM201
|
4.3
|
59.0
|
1.0
|
C2D
|
C:HEM201
|
4.4
|
57.8
|
1.0
|
C3D
|
C:HEM201
|
4.4
|
61.5
|
1.0
|
CG
|
C:HIS87
|
4.6
|
87.0
|
1.0
|
CG2
|
C:VAL62
|
4.6
|
72.1
|
1.0
|
|
Iron binding site 3 out
of 6 in 4n7o
Go back to
Iron Binding Sites List in 4n7o
Iron binding site 3 out
of 6 in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin with Phosphate at 2.5 A Resolution.
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin with Phosphate at 2.5 A Resolution. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Fe201
b:41.2
occ:1.00
|
FE
|
F:HEM201
|
0.0
|
41.2
|
1.0
|
NC
|
F:HEM201
|
2.0
|
37.2
|
1.0
|
NA
|
F:HEM201
|
2.0
|
41.2
|
1.0
|
NB
|
F:HEM201
|
2.0
|
37.7
|
1.0
|
NE2
|
F:HIS92
|
2.1
|
60.8
|
1.0
|
ND
|
F:HEM201
|
2.1
|
38.8
|
1.0
|
CE1
|
F:HIS92
|
3.0
|
60.0
|
1.0
|
C1B
|
F:HEM201
|
3.0
|
39.6
|
1.0
|
C4C
|
F:HEM201
|
3.0
|
36.2
|
1.0
|
C4A
|
F:HEM201
|
3.1
|
42.9
|
1.0
|
C1C
|
F:HEM201
|
3.1
|
37.2
|
1.0
|
C1A
|
F:HEM201
|
3.1
|
42.4
|
1.0
|
C4B
|
F:HEM201
|
3.1
|
38.0
|
1.0
|
C1D
|
F:HEM201
|
3.1
|
41.0
|
1.0
|
CD2
|
F:HIS92
|
3.1
|
61.3
|
1.0
|
C4D
|
F:HEM201
|
3.1
|
41.6
|
1.0
|
CHB
|
F:HEM201
|
3.4
|
40.5
|
1.0
|
CHD
|
F:HEM201
|
3.4
|
39.5
|
1.0
|
CHC
|
F:HEM201
|
3.4
|
37.8
|
1.0
|
CHA
|
F:HEM201
|
3.5
|
40.1
|
1.0
|
ND1
|
F:HIS92
|
4.1
|
62.1
|
1.0
|
CG
|
F:HIS92
|
4.2
|
60.8
|
1.0
|
C3C
|
F:HEM201
|
4.3
|
33.9
|
1.0
|
C2B
|
F:HEM201
|
4.3
|
38.8
|
1.0
|
C2C
|
F:HEM201
|
4.3
|
35.1
|
1.0
|
C2A
|
F:HEM201
|
4.3
|
45.3
|
1.0
|
C3A
|
F:HEM201
|
4.3
|
44.3
|
1.0
|
C3B
|
F:HEM201
|
4.3
|
39.6
|
1.0
|
C2D
|
F:HEM201
|
4.4
|
41.2
|
1.0
|
C3D
|
F:HEM201
|
4.4
|
43.9
|
1.0
|
NE2
|
F:HIS63
|
4.5
|
56.0
|
1.0
|
CG2
|
F:VAL67
|
4.6
|
42.0
|
1.0
|
|
Iron binding site 4 out
of 6 in 4n7o
Go back to
Iron Binding Sites List in 4n7o
Iron binding site 4 out
of 6 in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin with Phosphate at 2.5 A Resolution.
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin with Phosphate at 2.5 A Resolution. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Fe201
b:67.7
occ:1.00
|
FE
|
G:HEM201
|
0.0
|
67.7
|
1.0
|
NC
|
G:HEM201
|
2.0
|
68.7
|
1.0
|
NA
|
G:HEM201
|
2.0
|
71.6
|
1.0
|
NB
|
G:HEM201
|
2.1
|
68.0
|
1.0
|
ND
|
G:HEM201
|
2.1
|
70.9
|
1.0
|
NE2
|
G:HIS87
|
2.3
|
73.9
|
1.0
|
C4C
|
G:HEM201
|
3.0
|
68.9
|
1.0
|
C1B
|
G:HEM201
|
3.0
|
67.4
|
1.0
|
C4A
|
G:HEM201
|
3.1
|
72.4
|
1.0
|
C1A
|
G:HEM201
|
3.1
|
71.9
|
1.0
|
C1C
|
G:HEM201
|
3.1
|
66.6
|
1.0
|
C1D
|
G:HEM201
|
3.1
|
71.2
|
1.0
|
C4B
|
G:HEM201
|
3.1
|
66.3
|
1.0
|
C4D
|
G:HEM201
|
3.1
|
71.8
|
1.0
|
CE1
|
G:HIS87
|
3.3
|
73.8
|
1.0
|
CD2
|
G:HIS87
|
3.3
|
73.9
|
1.0
|
CHB
|
G:HEM201
|
3.4
|
71.1
|
1.0
|
CHD
|
G:HEM201
|
3.4
|
70.1
|
1.0
|
CHA
|
G:HEM201
|
3.5
|
71.3
|
1.0
|
CHC
|
G:HEM201
|
3.5
|
66.6
|
1.0
|
C3C
|
G:HEM201
|
4.3
|
67.7
|
1.0
|
C2C
|
G:HEM201
|
4.3
|
67.3
|
1.0
|
C3A
|
G:HEM201
|
4.3
|
72.1
|
1.0
|
C2A
|
G:HEM201
|
4.3
|
72.8
|
1.0
|
C2B
|
G:HEM201
|
4.3
|
64.4
|
1.0
|
C3B
|
G:HEM201
|
4.3
|
64.3
|
1.0
|
CE1
|
G:HIS58
|
4.3
|
73.4
|
1.0
|
C2D
|
G:HEM201
|
4.4
|
72.3
|
1.0
|
ND1
|
G:HIS87
|
4.4
|
72.4
|
1.0
|
C3D
|
G:HEM201
|
4.4
|
73.4
|
1.0
|
CG
|
G:HIS87
|
4.4
|
73.5
|
1.0
|
NE2
|
G:HIS58
|
4.5
|
74.4
|
1.0
|
CG2
|
G:VAL62
|
4.8
|
71.5
|
1.0
|
|
Iron binding site 5 out
of 6 in 4n7o
Go back to
Iron Binding Sites List in 4n7o
Iron binding site 5 out
of 6 in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin with Phosphate at 2.5 A Resolution.
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin with Phosphate at 2.5 A Resolution. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
J:Fe201
b:49.1
occ:1.00
|
FE
|
J:HEM201
|
0.0
|
49.1
|
1.0
|
NC
|
J:HEM201
|
2.0
|
53.2
|
1.0
|
NA
|
J:HEM201
|
2.1
|
53.3
|
1.0
|
NB
|
J:HEM201
|
2.1
|
52.8
|
1.0
|
ND
|
J:HEM201
|
2.1
|
53.1
|
1.0
|
NE2
|
J:HIS92
|
2.3
|
56.3
|
1.0
|
CE1
|
J:HIS92
|
3.0
|
55.7
|
1.0
|
C1B
|
J:HEM201
|
3.1
|
52.8
|
1.0
|
C4C
|
J:HEM201
|
3.1
|
52.3
|
1.0
|
C4A
|
J:HEM201
|
3.1
|
52.5
|
1.0
|
C1A
|
J:HEM201
|
3.1
|
54.6
|
1.0
|
C1C
|
J:HEM201
|
3.1
|
52.4
|
1.0
|
C1D
|
J:HEM201
|
3.1
|
54.0
|
1.0
|
C4B
|
J:HEM201
|
3.1
|
52.3
|
1.0
|
C4D
|
J:HEM201
|
3.1
|
55.3
|
1.0
|
CHB
|
J:HEM201
|
3.4
|
53.3
|
1.0
|
CHD
|
J:HEM201
|
3.4
|
53.0
|
1.0
|
CHA
|
J:HEM201
|
3.5
|
54.6
|
1.0
|
CHC
|
J:HEM201
|
3.5
|
51.5
|
1.0
|
CD2
|
J:HIS92
|
3.5
|
58.2
|
1.0
|
NE2
|
J:HIS63
|
4.1
|
43.6
|
1.0
|
CG2
|
J:VAL67
|
4.1
|
36.9
|
1.0
|
ND1
|
J:HIS92
|
4.2
|
58.5
|
1.0
|
C3C
|
J:HEM201
|
4.3
|
52.8
|
1.0
|
C3A
|
J:HEM201
|
4.3
|
55.7
|
1.0
|
C2A
|
J:HEM201
|
4.3
|
57.3
|
1.0
|
C2B
|
J:HEM201
|
4.3
|
52.3
|
1.0
|
C2C
|
J:HEM201
|
4.3
|
52.9
|
1.0
|
C3B
|
J:HEM201
|
4.4
|
51.9
|
1.0
|
C2D
|
J:HEM201
|
4.4
|
56.0
|
1.0
|
CE1
|
J:HIS63
|
4.4
|
43.4
|
1.0
|
C3D
|
J:HEM201
|
4.4
|
58.1
|
1.0
|
CG
|
J:HIS92
|
4.5
|
60.4
|
1.0
|
|
Iron binding site 6 out
of 6 in 4n7o
Go back to
Iron Binding Sites List in 4n7o
Iron binding site 6 out
of 6 in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin with Phosphate at 2.5 A Resolution.
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin with Phosphate at 2.5 A Resolution. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
K:Fe201
b:53.8
occ:1.00
|
FE
|
K:HEM201
|
0.0
|
53.8
|
1.0
|
NA
|
K:HEM201
|
2.0
|
53.3
|
1.0
|
NC
|
K:HEM201
|
2.1
|
53.6
|
1.0
|
NB
|
K:HEM201
|
2.1
|
51.2
|
1.0
|
ND
|
K:HEM201
|
2.1
|
53.2
|
1.0
|
C1B
|
K:HEM201
|
3.0
|
50.4
|
1.0
|
C4A
|
K:HEM201
|
3.1
|
53.2
|
1.0
|
C4C
|
K:HEM201
|
3.1
|
52.9
|
1.0
|
C1A
|
K:HEM201
|
3.1
|
54.2
|
1.0
|
NE2
|
K:HIS87
|
3.1
|
66.2
|
1.0
|
C1C
|
K:HEM201
|
3.1
|
53.0
|
1.0
|
C1D
|
K:HEM201
|
3.1
|
55.6
|
1.0
|
C4D
|
K:HEM201
|
3.1
|
55.3
|
1.0
|
C4B
|
K:HEM201
|
3.1
|
49.7
|
1.0
|
CHB
|
K:HEM201
|
3.4
|
51.2
|
1.0
|
CHD
|
K:HEM201
|
3.4
|
54.9
|
1.0
|
CHA
|
K:HEM201
|
3.4
|
55.2
|
1.0
|
CHC
|
K:HEM201
|
3.5
|
51.1
|
1.0
|
CE1
|
K:HIS87
|
3.7
|
66.5
|
1.0
|
CD2
|
K:HIS87
|
4.2
|
65.8
|
1.0
|
NE2
|
K:HIS58
|
4.3
|
72.9
|
1.0
|
C3A
|
K:HEM201
|
4.3
|
54.6
|
1.0
|
C2A
|
K:HEM201
|
4.3
|
55.2
|
1.0
|
C3C
|
K:HEM201
|
4.3
|
52.3
|
1.0
|
C2B
|
K:HEM201
|
4.3
|
50.5
|
1.0
|
C2C
|
K:HEM201
|
4.3
|
53.9
|
1.0
|
C3B
|
K:HEM201
|
4.3
|
49.3
|
1.0
|
C2D
|
K:HEM201
|
4.4
|
57.5
|
1.0
|
C3D
|
K:HEM201
|
4.4
|
58.3
|
1.0
|
CE1
|
K:HIS58
|
4.6
|
73.0
|
1.0
|
CG2
|
K:VAL62
|
4.7
|
63.3
|
1.0
|
ND1
|
K:HIS87
|
4.9
|
66.4
|
1.0
|
|
Reference:
N.Shibayama,
K.Sugiyama,
J.R.Tame,
S.Y.Park.
Capturing the Hemoglobin Allosteric Transition in A Single Crystal Form J.Am.Chem.Soc. V. 136 5097 2014.
ISSN: ISSN 0002-7863
PubMed: 24635037
DOI: 10.1021/JA500380E
Page generated: Mon Aug 5 07:16:16 2024
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