Atomistry » Nickel » PDB 4lto-4ofl » 4n7o
Atomistry »
  Nickel »
    PDB 4lto-4ofl »
      4n7o »

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:

Iron (Fe) 6 atoms

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

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy