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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:

Nickel (Ni) 6 atoms

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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