Nickel 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:
Nickel Binding Sites:
The binding sites of Nickel 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 Nickel atom.
In total 6 binding sites of Nickel 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 Nickel binding site number:
1;
2;
3;
4;
5;
6;
Nickel binding site 1 out
of 6 in 4n7o
Go back to
Nickel Binding Sites List in 4n7o
Nickel 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 Nickel with other atoms in the Ni 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
|
A:Ni201
b:69.3
occ:1.00
|
NI
|
A:HNI201
|
0.0
|
69.3
|
1.0
|
NC
|
A:HNI201
|
2.0
|
68.2
|
1.0
|
NA
|
A:HNI201
|
2.1
|
71.4
|
1.0
|
NB
|
A:HNI201
|
2.1
|
66.2
|
1.0
|
ND
|
A:HNI201
|
2.1
|
70.2
|
1.0
|
NE2
|
A:HIS87
|
2.3
|
90.3
|
1.0
|
C4C
|
A:HNI201
|
3.0
|
68.2
|
1.0
|
C1B
|
A:HNI201
|
3.1
|
65.8
|
1.0
|
CE1
|
A:HIS87
|
3.1
|
91.4
|
1.0
|
C4A
|
A:HNI201
|
3.1
|
70.3
|
1.0
|
C1D
|
A:HNI201
|
3.1
|
70.0
|
1.0
|
C1C
|
A:HNI201
|
3.1
|
66.7
|
1.0
|
C1A
|
A:HNI201
|
3.1
|
73.0
|
1.0
|
CD2
|
A:HIS87
|
3.1
|
89.8
|
1.0
|
C4B
|
A:HNI201
|
3.1
|
65.0
|
1.0
|
C4D
|
A:HNI201
|
3.1
|
71.5
|
1.0
|
CHD
|
A:HNI201
|
3.4
|
69.5
|
1.0
|
CHB
|
A:HNI201
|
3.4
|
68.4
|
1.0
|
CHA
|
A:HNI201
|
3.5
|
72.5
|
1.0
|
CHC
|
A:HNI201
|
3.5
|
65.3
|
1.0
|
ND1
|
A:HIS87
|
4.0
|
89.8
|
1.0
|
CG
|
A:HIS87
|
4.1
|
89.1
|
1.0
|
C3C
|
A:HNI201
|
4.3
|
67.1
|
1.0
|
C2C
|
A:HNI201
|
4.3
|
67.2
|
1.0
|
C3A
|
A:HNI201
|
4.3
|
72.2
|
1.0
|
C2A
|
A:HNI201
|
4.3
|
74.2
|
1.0
|
C2B
|
A:HNI201
|
4.3
|
63.6
|
1.0
|
C2D
|
A:HNI201
|
4.4
|
71.1
|
1.0
|
C3B
|
A:HNI201
|
4.4
|
62.8
|
1.0
|
C3D
|
A:HNI201
|
4.4
|
72.0
|
1.0
|
CG2
|
A:VAL62
|
4.8
|
65.7
|
1.0
|
|
Nickel binding site 2 out
of 6 in 4n7o
Go back to
Nickel Binding Sites List in 4n7o
Nickel 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 Nickel with other atoms in the Ni 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
|
D:Ni201
b:51.7
occ:1.00
|
NI
|
D:HNI201
|
0.0
|
51.7
|
1.0
|
NC
|
D:HNI201
|
2.0
|
48.5
|
1.0
|
NB
|
D:HNI201
|
2.1
|
48.9
|
1.0
|
NA
|
D:HNI201
|
2.1
|
51.6
|
1.0
|
ND
|
D:HNI201
|
2.1
|
50.3
|
1.0
|
NE2
|
D:HIS92
|
2.3
|
69.6
|
1.0
|
C4C
|
D:HNI201
|
3.0
|
48.5
|
1.0
|
CD2
|
D:HIS92
|
3.0
|
69.7
|
1.0
|
C1B
|
D:HNI201
|
3.1
|
49.1
|
1.0
|
C1D
|
D:HNI201
|
3.1
|
50.7
|
1.0
|
C1C
|
D:HNI201
|
3.1
|
47.4
|
1.0
|
C4A
|
D:HNI201
|
3.1
|
53.5
|
1.0
|
C1A
|
D:HNI201
|
3.1
|
51.8
|
1.0
|
C4D
|
D:HNI201
|
3.1
|
52.9
|
1.0
|
C4B
|
D:HNI201
|
3.1
|
48.5
|
1.0
|
CHD
|
D:HNI201
|
3.4
|
49.6
|
1.0
|
CHB
|
D:HNI201
|
3.4
|
52.3
|
1.0
|
CHA
|
D:HNI201
|
3.4
|
51.1
|
1.0
|
CHC
|
D:HNI201
|
3.5
|
48.7
|
1.0
|
CE1
|
D:HIS92
|
3.5
|
69.1
|
1.0
|
CG
|
D:HIS92
|
4.3
|
70.1
|
1.0
|
NE2
|
D:HIS63
|
4.3
|
74.4
|
1.0
|
C3C
|
D:HNI201
|
4.3
|
46.4
|
1.0
|
C2C
|
D:HNI201
|
4.3
|
47.8
|
1.0
|
C3A
|
D:HNI201
|
4.3
|
55.0
|
1.0
|
C2B
|
D:HNI201
|
4.3
|
49.1
|
1.0
|
C2A
|
D:HNI201
|
4.3
|
55.8
|
1.0
|
C2D
|
D:HNI201
|
4.3
|
52.0
|
1.0
|
C3B
|
D:HNI201
|
4.4
|
49.1
|
1.0
|
C3D
|
D:HNI201
|
4.4
|
54.8
|
1.0
|
ND1
|
D:HIS92
|
4.5
|
69.5
|
1.0
|
CG2
|
D:VAL67
|
4.5
|
61.3
|
1.0
|
CD2
|
D:HIS63
|
4.9
|
74.5
|
1.0
|
|
Nickel binding site 3 out
of 6 in 4n7o
Go back to
Nickel Binding Sites List in 4n7o
Nickel 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 Nickel with other atoms in the Ni 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
|
E:Ni201
b:50.8
occ:1.00
|
NI
|
E:HNI201
|
0.0
|
50.8
|
1.0
|
NC
|
E:HNI201
|
2.0
|
53.4
|
1.0
|
NA
|
E:HNI201
|
2.1
|
56.2
|
1.0
|
NB
|
E:HNI201
|
2.1
|
54.5
|
1.0
|
ND
|
E:HNI201
|
2.1
|
57.9
|
1.0
|
NE2
|
E:HIS87
|
2.2
|
66.0
|
1.0
|
CE1
|
E:HIS87
|
2.9
|
66.2
|
1.0
|
C4C
|
E:HNI201
|
3.0
|
52.5
|
1.0
|
C1B
|
E:HNI201
|
3.1
|
54.8
|
1.0
|
C1C
|
E:HNI201
|
3.1
|
51.8
|
1.0
|
C1D
|
E:HNI201
|
3.1
|
57.4
|
1.0
|
C4A
|
E:HNI201
|
3.1
|
57.0
|
1.0
|
C4B
|
E:HNI201
|
3.1
|
52.7
|
1.0
|
C1A
|
E:HNI201
|
3.1
|
58.0
|
1.0
|
C4D
|
E:HNI201
|
3.1
|
59.2
|
1.0
|
CD2
|
E:HIS87
|
3.3
|
65.6
|
1.0
|
CHD
|
E:HNI201
|
3.4
|
54.9
|
1.0
|
CHB
|
E:HNI201
|
3.4
|
56.2
|
1.0
|
CHC
|
E:HNI201
|
3.5
|
51.7
|
1.0
|
CHA
|
E:HNI201
|
3.5
|
59.4
|
1.0
|
ND1
|
E:HIS87
|
4.1
|
66.3
|
1.0
|
CG
|
E:HIS87
|
4.3
|
65.7
|
1.0
|
C3C
|
E:HNI201
|
4.3
|
50.1
|
1.0
|
NE2
|
E:HIS58
|
4.3
|
69.2
|
1.0
|
C2C
|
E:HNI201
|
4.3
|
51.8
|
1.0
|
C2B
|
E:HNI201
|
4.3
|
54.7
|
1.0
|
C3A
|
E:HNI201
|
4.3
|
58.9
|
1.0
|
C3B
|
E:HNI201
|
4.4
|
55.5
|
1.0
|
C2A
|
E:HNI201
|
4.4
|
59.1
|
1.0
|
C2D
|
E:HNI201
|
4.4
|
58.6
|
1.0
|
C3D
|
E:HNI201
|
4.4
|
60.1
|
1.0
|
CG2
|
E:VAL62
|
4.9
|
47.5
|
1.0
|
|
Nickel binding site 4 out
of 6 in 4n7o
Go back to
Nickel Binding Sites List in 4n7o
Nickel 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 Nickel with other atoms in the Ni 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
|
H:Ni201
b:56.6
occ:1.00
|
NI
|
H:HNI201
|
0.0
|
56.6
|
1.0
|
NC
|
H:HNI201
|
2.0
|
58.7
|
1.0
|
NA
|
H:HNI201
|
2.1
|
60.0
|
1.0
|
NB
|
H:HNI201
|
2.1
|
58.1
|
1.0
|
ND
|
H:HNI201
|
2.1
|
59.0
|
1.0
|
NE2
|
H:HIS92
|
2.2
|
61.9
|
1.0
|
C4C
|
H:HNI201
|
3.0
|
58.0
|
1.0
|
C1B
|
H:HNI201
|
3.1
|
59.1
|
1.0
|
CE1
|
H:HIS92
|
3.1
|
63.1
|
1.0
|
C4A
|
H:HNI201
|
3.1
|
60.2
|
1.0
|
C1A
|
H:HNI201
|
3.1
|
60.7
|
1.0
|
C1C
|
H:HNI201
|
3.1
|
56.6
|
1.0
|
C1D
|
H:HNI201
|
3.1
|
59.6
|
1.0
|
C4B
|
H:HNI201
|
3.1
|
57.3
|
1.0
|
C4D
|
H:HNI201
|
3.1
|
60.4
|
1.0
|
CD2
|
H:HIS92
|
3.2
|
63.9
|
1.0
|
CHB
|
H:HNI201
|
3.4
|
60.4
|
1.0
|
CHD
|
H:HNI201
|
3.4
|
59.6
|
1.0
|
CHA
|
H:HNI201
|
3.5
|
60.1
|
1.0
|
CHC
|
H:HNI201
|
3.5
|
56.3
|
1.0
|
ND1
|
H:HIS92
|
4.2
|
62.1
|
1.0
|
NE2
|
H:HIS63
|
4.3
|
57.8
|
1.0
|
CG
|
H:HIS92
|
4.3
|
64.4
|
1.0
|
C3C
|
H:HNI201
|
4.3
|
56.7
|
1.0
|
C3A
|
H:HNI201
|
4.3
|
62.1
|
1.0
|
C2A
|
H:HNI201
|
4.3
|
63.0
|
1.0
|
C2C
|
H:HNI201
|
4.3
|
56.5
|
1.0
|
C2B
|
H:HNI201
|
4.3
|
59.6
|
1.0
|
C3B
|
H:HNI201
|
4.4
|
58.7
|
1.0
|
C2D
|
H:HNI201
|
4.4
|
60.9
|
1.0
|
C3D
|
H:HNI201
|
4.4
|
62.2
|
1.0
|
CG2
|
H:VAL67
|
4.7
|
60.6
|
1.0
|
|
Nickel binding site 5 out
of 6 in 4n7o
Go back to
Nickel Binding Sites List in 4n7o
Nickel 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 Nickel with other atoms in the Ni 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
|
I:Ni201
b:55.0
occ:1.00
|
NI
|
I:HNI201
|
0.0
|
55.0
|
1.0
|
NC
|
I:HNI201
|
2.1
|
57.5
|
1.0
|
NA
|
I:HNI201
|
2.1
|
59.9
|
1.0
|
NB
|
I:HNI201
|
2.1
|
55.8
|
1.0
|
ND
|
I:HNI201
|
2.1
|
57.3
|
1.0
|
NE2
|
I:HIS87
|
2.9
|
82.6
|
1.0
|
C4C
|
I:HNI201
|
3.0
|
56.4
|
1.0
|
C1B
|
I:HNI201
|
3.1
|
56.9
|
1.0
|
C1D
|
I:HNI201
|
3.1
|
59.7
|
1.0
|
C4A
|
I:HNI201
|
3.1
|
59.7
|
1.0
|
C1A
|
I:HNI201
|
3.1
|
60.5
|
1.0
|
C4D
|
I:HNI201
|
3.1
|
59.1
|
1.0
|
C1C
|
I:HNI201
|
3.1
|
55.1
|
1.0
|
C4B
|
I:HNI201
|
3.1
|
56.5
|
1.0
|
CE1
|
I:HIS87
|
3.3
|
82.5
|
1.0
|
CHD
|
I:HNI201
|
3.4
|
59.7
|
1.0
|
CHB
|
I:HNI201
|
3.4
|
59.3
|
1.0
|
CHA
|
I:HNI201
|
3.4
|
60.4
|
1.0
|
CHC
|
I:HNI201
|
3.5
|
54.8
|
1.0
|
CD2
|
I:HIS87
|
4.1
|
81.7
|
1.0
|
C3C
|
I:HNI201
|
4.3
|
55.6
|
1.0
|
NE2
|
I:HIS58
|
4.3
|
60.3
|
1.0
|
C2D
|
I:HNI201
|
4.3
|
59.9
|
1.0
|
C2B
|
I:HNI201
|
4.3
|
55.3
|
1.0
|
C3A
|
I:HNI201
|
4.3
|
61.6
|
1.0
|
C2A
|
I:HNI201
|
4.3
|
62.7
|
1.0
|
C2C
|
I:HNI201
|
4.3
|
56.3
|
1.0
|
C3D
|
I:HNI201
|
4.4
|
60.5
|
1.0
|
C3B
|
I:HNI201
|
4.4
|
55.4
|
1.0
|
CG2
|
I:VAL62
|
4.5
|
51.5
|
1.0
|
ND1
|
I:HIS87
|
4.6
|
82.1
|
1.0
|
CE1
|
I:HIS58
|
5.0
|
59.9
|
1.0
|
|
Nickel binding site 6 out
of 6 in 4n7o
Go back to
Nickel Binding Sites List in 4n7o
Nickel 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 Nickel with other atoms in the Ni 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
|
L:Ni201
b:65.4
occ:1.00
|
NI
|
L:HNI201
|
0.0
|
65.4
|
1.0
|
NC
|
L:HNI201
|
2.0
|
66.7
|
1.0
|
NA
|
L:HNI201
|
2.1
|
68.4
|
1.0
|
NB
|
L:HNI201
|
2.1
|
65.2
|
1.0
|
ND
|
L:HNI201
|
2.1
|
67.8
|
1.0
|
NE2
|
L:HIS92
|
2.4
|
80.2
|
1.0
|
C1B
|
L:HNI201
|
3.1
|
65.0
|
1.0
|
C4C
|
L:HNI201
|
3.1
|
66.1
|
1.0
|
C4A
|
L:HNI201
|
3.1
|
68.3
|
1.0
|
C1A
|
L:HNI201
|
3.1
|
69.4
|
1.0
|
C1C
|
L:HNI201
|
3.1
|
66.9
|
1.0
|
C1D
|
L:HNI201
|
3.1
|
68.2
|
1.0
|
C4D
|
L:HNI201
|
3.1
|
69.5
|
1.0
|
C4B
|
L:HNI201
|
3.1
|
65.7
|
1.0
|
CD2
|
L:HIS92
|
3.4
|
80.6
|
1.0
|
CE1
|
L:HIS92
|
3.4
|
80.7
|
1.0
|
CHB
|
L:HNI201
|
3.4
|
66.7
|
1.0
|
CHD
|
L:HNI201
|
3.4
|
67.2
|
1.0
|
CHA
|
L:HNI201
|
3.5
|
69.4
|
1.0
|
CHC
|
L:HNI201
|
3.5
|
66.6
|
1.0
|
CG2
|
L:VAL67
|
4.0
|
58.1
|
1.0
|
NE2
|
L:HIS63
|
4.1
|
77.5
|
1.0
|
C3A
|
L:HNI201
|
4.3
|
68.8
|
1.0
|
C2A
|
L:HNI201
|
4.3
|
70.3
|
1.0
|
C2C
|
L:HNI201
|
4.3
|
65.8
|
1.0
|
C3C
|
L:HNI201
|
4.3
|
65.8
|
1.0
|
C2B
|
L:HNI201
|
4.3
|
65.2
|
1.0
|
C2D
|
L:HNI201
|
4.4
|
70.8
|
1.0
|
C3B
|
L:HNI201
|
4.4
|
64.9
|
1.0
|
C3D
|
L:HNI201
|
4.4
|
71.7
|
1.0
|
ND1
|
L:HIS92
|
4.5
|
81.9
|
1.0
|
CG
|
L:HIS92
|
4.5
|
82.0
|
1.0
|
CD2
|
L:HIS63
|
5.0
|
76.2
|
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: Wed Oct 9 18:33:43 2024
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