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Iron in PDB 3wct: The Structure of A Deoxygenated 400 kDa Hemoglobin Provides A More Accurate Description of the Cooperative Mechanism of Giant Hemoglobins: Oxygenated 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: Oxygenated Form, PDB code: 3wct 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) 43.02 / 2.40
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 108.556, 108.556, 193.552, 90.00, 90.00, 120.00
R / Rfree (%) 21.6 / 26.4

Other elements in 3wct:

The structure of The Structure of A Deoxygenated 400 kDa Hemoglobin Provides A More Accurate Description of the Cooperative Mechanism of Giant Hemoglobins: Oxygenated Form also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

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: Oxygenated Form (pdb code 3wct). 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: Oxygenated Form, PDB code: 3wct:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Iron binding site 1 out of 8 in 3wct

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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: Oxygenated 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: Oxygenated Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe200

b:38.3
occ:1.00
FE A:HEM200 0.0 38.3 1.0
O1 A:OXY201 1.8 50.8 1.0
NA A:HEM200 2.0 36.0 1.0
NC A:HEM200 2.0 34.8 1.0
NB A:HEM200 2.0 35.3 1.0
ND A:HEM200 2.0 37.0 1.0
NE2 A:HIS94 2.1 46.1 1.0
O2 A:OXY201 2.8 56.5 1.0
C4C A:HEM200 3.0 35.5 1.0
C1D A:HEM200 3.0 34.6 1.0
C1B A:HEM200 3.0 34.4 1.0
C1C A:HEM200 3.0 35.9 1.0
C4A A:HEM200 3.0 35.5 1.0
C4D A:HEM200 3.0 39.5 1.0
C1A A:HEM200 3.0 37.3 1.0
CE1 A:HIS94 3.1 48.0 1.0
C4B A:HEM200 3.1 32.6 1.0
CD2 A:HIS94 3.2 44.8 1.0
CHB A:HEM200 3.4 34.0 1.0
CHD A:HEM200 3.4 33.8 1.0
CHA A:HEM200 3.4 38.3 1.0
CHC A:HEM200 3.4 35.1 1.0
ND1 A:HIS94 4.2 45.6 1.0
C3A A:HEM200 4.2 35.1 1.0
C2A A:HEM200 4.3 36.7 1.0
CG A:HIS94 4.3 45.3 1.0
C2B A:HEM200 4.3 33.7 1.0
C3B A:HEM200 4.3 32.1 1.0
C2C A:HEM200 4.3 35.2 1.0
C3D A:HEM200 4.3 39.1 1.0
C2D A:HEM200 4.3 37.1 1.0
C3C A:HEM200 4.3 35.4 1.0
CG2 A:VAL66 4.5 37.6 1.0
CE1 A:HIS62 4.7 33.2 1.0

Iron binding site 2 out of 8 in 3wct

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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: Oxygenated 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: Oxygenated Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe201

b:40.4
occ:1.00
FE B:HEM201 0.0 40.4 1.0
O1 B:OXY202 1.8 50.9 1.0
NA B:HEM201 2.0 38.0 1.0
NC B:HEM201 2.0 39.0 1.0
ND B:HEM201 2.0 40.9 1.0
NB B:HEM201 2.0 38.0 1.0
NE2 B:HIS95 2.1 51.3 1.0
O2 B:OXY202 2.8 54.3 1.0
C1D B:HEM201 3.0 41.2 1.0
C4C B:HEM201 3.0 41.1 1.0
C1C B:HEM201 3.0 40.6 1.0
C4D B:HEM201 3.0 39.8 1.0
C1B B:HEM201 3.0 37.2 1.0
C1A B:HEM201 3.0 39.1 1.0
C4A B:HEM201 3.0 37.4 1.0
CE1 B:HIS95 3.0 52.9 1.0
C4B B:HEM201 3.1 39.9 1.0
CD2 B:HIS95 3.1 53.1 1.0
CHB B:HEM201 3.4 36.1 1.0
CHD B:HEM201 3.4 40.1 1.0
CHA B:HEM201 3.4 38.9 1.0
CHC B:HEM201 3.4 39.3 1.0
ND1 B:HIS95 4.2 54.4 1.0
CG B:HIS95 4.2 56.4 1.0
C3A B:HEM201 4.3 36.9 1.0
C2A B:HEM201 4.3 37.5 1.0
C2C B:HEM201 4.3 39.5 1.0
C2B B:HEM201 4.3 38.5 1.0
C3D B:HEM201 4.3 39.5 1.0
C3B B:HEM201 4.3 40.5 1.0
C2D B:HEM201 4.3 40.5 1.0
C3C B:HEM201 4.3 41.1 1.0
CG2 B:VAL67 4.6 35.4 1.0
CE1 B:HIS63 4.7 32.4 1.0

Iron binding site 3 out of 8 in 3wct

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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: Oxygenated 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: Oxygenated Form within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe200

b:42.8
occ:1.00
FE C:HEM200 0.0 42.8 1.0
O1 C:OXY201 1.8 46.2 1.0
NA C:HEM200 2.0 42.1 1.0
NC C:HEM200 2.0 43.3 1.0
ND C:HEM200 2.0 44.2 1.0
NB C:HEM200 2.0 43.8 1.0
NE2 C:HIS99 2.1 47.6 1.0
CD2 C:HIS99 2.9 48.8 1.0
O2 C:OXY201 2.9 50.5 1.0
C4C C:HEM200 3.0 45.3 1.0
C1D C:HEM200 3.0 42.4 1.0
C4D C:HEM200 3.0 42.7 1.0
C1C C:HEM200 3.0 45.1 1.0
C1B C:HEM200 3.0 41.4 1.0
C4A C:HEM200 3.0 40.2 1.0
C1A C:HEM200 3.0 42.7 1.0
C4B C:HEM200 3.1 42.6 1.0
CE1 C:HIS99 3.2 49.2 1.0
CHD C:HEM200 3.4 43.1 1.0
CHB C:HEM200 3.4 39.1 1.0
CHA C:HEM200 3.4 42.9 1.0
CHC C:HEM200 3.4 44.2 1.0
CG C:HIS99 4.1 50.3 1.0
ND1 C:HIS99 4.2 48.8 1.0
C3A C:HEM200 4.3 41.6 1.0
C2A C:HEM200 4.3 42.5 1.0
C3D C:HEM200 4.3 45.2 1.0
C2C C:HEM200 4.3 44.0 1.0
C2B C:HEM200 4.3 43.6 1.0
C3B C:HEM200 4.3 43.6 1.0
C2D C:HEM200 4.3 45.4 1.0
C3C C:HEM200 4.3 46.6 1.0
CG2 C:VAL71 4.8 34.8 1.0
CE1 C:HIS67 4.9 36.2 1.0

Iron binding site 4 out of 8 in 3wct

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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: Oxygenated 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: Oxygenated Form within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe201

b:49.9
occ:1.00
FE D:HEM201 0.0 49.9 1.0
O1 D:OXY202 1.8 53.4 1.0
NA D:HEM201 2.0 51.4 1.0
ND D:HEM201 2.0 53.2 1.0
NC D:HEM201 2.0 52.3 1.0
NB D:HEM201 2.0 51.3 1.0
NE2 D:HIS99 2.1 55.3 1.0
O2 D:OXY202 2.7 59.1 1.0
CE1 D:HIS99 3.0 59.2 1.0
C1D D:HEM201 3.0 53.0 1.0
C4C D:HEM201 3.0 52.0 1.0
C4D D:HEM201 3.0 54.2 1.0
C4A D:HEM201 3.0 48.7 1.0
C1B D:HEM201 3.0 49.6 1.0
C1A D:HEM201 3.0 50.9 1.0
C1C D:HEM201 3.0 51.1 1.0
C4B D:HEM201 3.1 50.5 1.0
CD2 D:HIS99 3.1 58.0 1.0
CHB D:HEM201 3.3 48.6 1.0
CHD D:HEM201 3.4 52.8 1.0
CHA D:HEM201 3.4 52.5 1.0
CHC D:HEM201 3.4 50.3 1.0
ND1 D:HIS99 4.1 57.7 1.0
CG D:HIS99 4.2 58.4 1.0
C3A D:HEM201 4.2 48.6 1.0
C2A D:HEM201 4.2 50.6 1.0
C3D D:HEM201 4.3 55.8 1.0
C2B D:HEM201 4.3 51.2 1.0
C2D D:HEM201 4.3 55.5 1.0
C3B D:HEM201 4.3 51.3 1.0
C2C D:HEM201 4.3 51.5 1.0
C3C D:HEM201 4.3 53.2 1.0
CG2 D:VAL71 4.7 38.9 1.0
CE1 D:HIS67 4.9 39.0 1.0

Iron binding site 5 out of 8 in 3wct

Go back to Iron Binding Sites List in 3wct
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: Oxygenated 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: Oxygenated Form within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe200

b:44.3
occ:1.00
FE E:HEM200 0.0 44.3 1.0
O1 E:OXY201 1.8 53.2 1.0
NC E:HEM200 2.0 41.5 1.0
NB E:HEM200 2.0 43.5 1.0
NA E:HEM200 2.0 44.2 1.0
ND E:HEM200 2.0 44.9 1.0
NE2 E:HIS94 2.1 48.9 1.0
O2 E:OXY201 2.8 57.9 1.0
C4C E:HEM200 3.0 42.8 1.0
C1C E:HEM200 3.0 43.0 1.0
C1D E:HEM200 3.0 44.0 1.0
C1B E:HEM200 3.0 43.4 1.0
C4D E:HEM200 3.0 43.5 1.0
C1A E:HEM200 3.1 45.5 1.0
C4B E:HEM200 3.1 43.2 1.0
C4A E:HEM200 3.1 44.8 1.0
CD2 E:HIS94 3.1 49.9 1.0
CE1 E:HIS94 3.1 50.5 1.0
CHD E:HEM200 3.4 42.5 1.0
CHB E:HEM200 3.4 44.2 1.0
CHA E:HEM200 3.4 45.4 1.0
CHC E:HEM200 3.4 43.9 1.0
ND1 E:HIS94 4.2 51.4 1.0
CG E:HIS94 4.2 51.0 1.0
C3A E:HEM200 4.3 47.1 1.0
C2A E:HEM200 4.3 46.7 1.0
C3B E:HEM200 4.3 43.5 1.0
C2C E:HEM200 4.3 43.0 1.0
C2B E:HEM200 4.3 44.7 1.0
C3D E:HEM200 4.3 43.2 1.0
C3C E:HEM200 4.3 44.5 1.0
C2D E:HEM200 4.3 43.7 1.0
CG2 E:VAL66 4.6 41.3 1.0
CE1 E:HIS62 4.8 35.6 1.0

Iron binding site 6 out of 8 in 3wct

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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: Oxygenated 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: Oxygenated Form within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe201

b:39.4
occ:1.00
FE F:HEM201 0.0 39.4 1.0
O1 F:OXY202 1.8 48.2 1.0
NC F:HEM201 2.0 35.4 1.0
NA F:HEM201 2.0 36.9 1.0
NB F:HEM201 2.0 37.0 1.0
ND F:HEM201 2.0 38.3 1.0
NE2 F:HIS95 2.1 45.8 1.0
O2 F:OXY202 2.9 48.3 1.0
C4C F:HEM201 3.0 36.1 1.0
CE1 F:HIS95 3.0 45.8 1.0
C1D F:HEM201 3.0 37.0 1.0
C1C F:HEM201 3.0 37.3 1.0
C1B F:HEM201 3.0 39.0 1.0
C4D F:HEM201 3.0 37.9 1.0
C4A F:HEM201 3.0 36.6 1.0
C1A F:HEM201 3.0 38.0 1.0
C4B F:HEM201 3.1 38.1 1.0
CD2 F:HIS95 3.1 46.8 1.0
CHB F:HEM201 3.4 35.5 1.0
CHD F:HEM201 3.4 35.8 1.0
CHA F:HEM201 3.4 38.5 1.0
CHC F:HEM201 3.4 36.7 1.0
ND1 F:HIS95 4.1 47.2 1.0
CG F:HIS95 4.2 48.6 1.0
C3A F:HEM201 4.3 36.4 1.0
C2C F:HEM201 4.3 37.0 1.0
C2A F:HEM201 4.3 37.6 1.0
C3D F:HEM201 4.3 37.7 1.0
C2B F:HEM201 4.3 38.6 1.0
C3B F:HEM201 4.3 39.0 1.0
C3C F:HEM201 4.3 36.3 1.0
C2D F:HEM201 4.3 39.0 1.0
CG2 F:VAL67 4.7 26.7 1.0
CE1 F:HIS63 4.9 27.2 1.0

Iron binding site 7 out of 8 in 3wct

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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: Oxygenated 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: Oxygenated Form within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Fe200

b:40.0
occ:1.00
FE G:HEM200 0.0 40.0 1.0
O1 G:OXY201 1.8 47.8 1.0
ND G:HEM200 2.0 43.5 1.0
NC G:HEM200 2.0 41.0 1.0
NA G:HEM200 2.0 40.3 1.0
NB G:HEM200 2.0 40.7 1.0
NE2 G:HIS99 2.1 48.7 1.0
O2 G:OXY201 2.8 50.1 1.0
CE1 G:HIS99 3.0 50.8 1.0
C1D G:HEM200 3.0 42.6 1.0
C4C G:HEM200 3.0 41.7 1.0
C4D G:HEM200 3.0 43.9 1.0
C1C G:HEM200 3.0 41.4 1.0
C1B G:HEM200 3.0 38.9 1.0
C1A G:HEM200 3.1 41.5 1.0
C4A G:HEM200 3.1 37.9 1.0
C4B G:HEM200 3.1 40.6 1.0
CD2 G:HIS99 3.1 50.9 1.0
CHD G:HEM200 3.4 41.2 1.0
CHB G:HEM200 3.4 39.1 1.0
CHA G:HEM200 3.4 43.7 1.0
CHC G:HEM200 3.4 40.3 1.0
ND1 G:HIS99 4.1 49.7 1.0
CG G:HIS99 4.2 50.8 1.0
C3A G:HEM200 4.3 41.3 1.0
C3D G:HEM200 4.3 42.7 1.0
C2A G:HEM200 4.3 40.3 1.0
C2C G:HEM200 4.3 40.2 1.0
C2D G:HEM200 4.3 43.7 1.0
C2B G:HEM200 4.3 38.3 1.0
C3B G:HEM200 4.3 39.1 1.0
C3C G:HEM200 4.3 42.4 1.0
CE1 G:HIS67 4.6 35.2 1.0
CG2 G:VAL71 4.7 38.3 1.0

Iron binding site 8 out of 8 in 3wct

Go back to Iron Binding Sites List in 3wct
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: Oxygenated 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: Oxygenated Form within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Fe201

b:47.8
occ:1.00
FE H:HEM201 0.0 47.8 1.0
O1 H:OXY202 1.8 52.0 1.0
NA H:HEM201 2.0 48.9 1.0
NC H:HEM201 2.0 46.7 1.0
ND H:HEM201 2.0 48.4 1.0
NB H:HEM201 2.0 48.0 1.0
NE2 H:HIS99 2.1 55.4 1.0
O2 H:OXY202 2.8 55.4 1.0
C1D H:HEM201 3.0 47.1 1.0
C4C H:HEM201 3.0 46.5 1.0
CE1 H:HIS99 3.0 56.1 1.0
C4D H:HEM201 3.0 48.6 1.0
C1C H:HEM201 3.0 46.2 1.0
C4A H:HEM201 3.0 48.2 1.0
C1B H:HEM201 3.0 45.6 1.0
C1A H:HEM201 3.1 49.6 1.0
C4B H:HEM201 3.1 46.6 1.0
CD2 H:HIS99 3.1 59.1 1.0
CHD H:HEM201 3.4 46.7 1.0
CHB H:HEM201 3.4 46.2 1.0
CHA H:HEM201 3.4 49.5 1.0
CHC H:HEM201 3.4 46.7 1.0
ND1 H:HIS99 4.1 58.0 1.0
CG H:HIS99 4.2 60.5 1.0
C3A H:HEM201 4.3 49.5 1.0
C2A H:HEM201 4.3 50.9 1.0
C3D H:HEM201 4.3 49.0 1.0
C2C H:HEM201 4.3 45.9 1.0
C2D H:HEM201 4.3 49.1 1.0
C3B H:HEM201 4.3 46.1 1.0
C2B H:HEM201 4.3 46.7 1.0
C3C H:HEM201 4.3 46.5 1.0
CG2 H:VAL71 4.6 40.9 1.0
CE1 H:HIS67 5.0 37.8 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 22:35:11 2024

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