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Iron in PDB 3wcv: The Structure of A Deoxygenated 400 kDa Hemoglobin Provides A More Accurate Description of the Cooperative Mechanism of Giant Hemoglobins: Ca Bound 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: Ca Bound Form, PDB code: 3wcv 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) 36.33 / 2.60
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 108.944, 108.944, 195.016, 90.00, 90.00, 120.00
R / Rfree (%) 23.5 / 26.7

Other elements in 3wcv:

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

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

Iron binding site 1 out of 8 in 3wcv

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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: Ca Bound 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: Ca Bound Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe201

b:31.9
occ:1.00
FE A:HEM201 0.0 31.9 1.0
O1 A:OXY202 1.9 41.3 1.0
NA A:HEM201 2.0 37.2 1.0
NC A:HEM201 2.0 36.5 1.0
NB A:HEM201 2.0 35.6 1.0
ND A:HEM201 2.0 38.5 1.0
NE2 A:HIS94 2.1 38.7 1.0
O2 A:OXY202 2.8 40.8 1.0
C4A A:HEM201 3.0 40.4 1.0
C4C A:HEM201 3.0 36.8 1.0
C1B A:HEM201 3.0 36.0 1.0
C1C A:HEM201 3.0 37.7 1.0
C1D A:HEM201 3.0 37.4 1.0
C4D A:HEM201 3.0 37.5 1.0
C1A A:HEM201 3.0 39.0 1.0
C4B A:HEM201 3.1 37.1 1.0
CD2 A:HIS94 3.1 39.7 1.0
CE1 A:HIS94 3.1 38.5 1.0
CHB A:HEM201 3.3 38.0 1.0
CHA A:HEM201 3.4 38.9 1.0
CHD A:HEM201 3.4 37.2 1.0
CHC A:HEM201 3.4 36.9 1.0
ND1 A:HIS94 4.2 39.5 1.0
CG A:HIS94 4.3 40.5 1.0
C3A A:HEM201 4.3 41.0 1.0
C2A A:HEM201 4.3 42.5 1.0
C2B A:HEM201 4.3 36.4 1.0
C3B A:HEM201 4.3 37.1 1.0
C2C A:HEM201 4.3 39.3 1.0
C3D A:HEM201 4.3 37.4 1.0
C3C A:HEM201 4.4 40.3 1.0
C2D A:HEM201 4.4 37.7 1.0
CG2 A:VAL66 4.6 35.8 1.0
CE1 A:HIS62 4.8 40.6 1.0

Iron binding site 2 out of 8 in 3wcv

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

b:65.2
occ:1.00
FE B:HEM201 0.0 65.2 1.0
O1 B:OXY202 1.8 70.9 1.0
NC B:HEM201 2.0 63.5 1.0
NA B:HEM201 2.0 63.0 1.0
ND B:HEM201 2.0 64.0 1.0
NB B:HEM201 2.0 62.0 1.0
NE2 B:HIS95 2.1 79.5 1.0
O2 B:OXY202 2.9 70.4 1.0
C1D B:HEM201 3.0 63.7 1.0
C4C B:HEM201 3.0 63.9 1.0
C4D B:HEM201 3.0 64.2 1.0
C1C B:HEM201 3.0 62.2 1.0
C1B B:HEM201 3.0 60.3 1.0
C1A B:HEM201 3.0 63.8 1.0
C4A B:HEM201 3.1 62.8 1.0
C4B B:HEM201 3.1 61.7 1.0
CE1 B:HIS95 3.1 83.6 1.0
CD2 B:HIS95 3.1 83.8 1.0
CHA B:HEM201 3.4 64.1 1.0
CHD B:HEM201 3.4 63.1 1.0
CHB B:HEM201 3.4 59.8 1.0
CHC B:HEM201 3.4 62.0 1.0
ND1 B:HIS95 4.2 84.2 1.0
CG B:HIS95 4.2 84.9 1.0
C2A B:HEM201 4.3 64.7 1.0
C3A B:HEM201 4.3 63.5 1.0
C3D B:HEM201 4.3 62.6 1.0
C2C B:HEM201 4.3 62.4 1.0
C2D B:HEM201 4.3 63.0 1.0
C2B B:HEM201 4.3 60.6 1.0
C3C B:HEM201 4.3 63.1 1.0
C3B B:HEM201 4.3 60.3 1.0
CG2 B:VAL67 4.5 46.5 1.0
CE1 B:HIS63 4.8 63.0 1.0

Iron binding site 3 out of 8 in 3wcv

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

b:69.1
occ:1.00
FE C:HEM200 0.0 69.1 1.0
O1 C:OXY201 1.8 78.7 1.0
NA C:HEM200 2.0 69.3 1.0
NC C:HEM200 2.0 68.5 1.0
ND C:HEM200 2.0 71.3 1.0
NB C:HEM200 2.0 70.3 1.0
NE2 C:HIS99 2.1 77.1 1.0
O2 C:OXY201 3.0 84.7 1.0
CD2 C:HIS99 3.0 79.4 1.0
C1D C:HEM200 3.0 71.2 1.0
C4C C:HEM200 3.0 70.1 1.0
C4D C:HEM200 3.0 72.3 1.0
C1C C:HEM200 3.0 68.6 1.0
C1B C:HEM200 3.0 69.2 1.0
C4A C:HEM200 3.0 69.1 1.0
C1A C:HEM200 3.1 70.3 1.0
C4B C:HEM200 3.1 69.2 1.0
CE1 C:HIS99 3.1 78.7 1.0
CHB C:HEM200 3.4 68.5 1.0
CHD C:HEM200 3.4 71.0 1.0
CHA C:HEM200 3.4 71.4 1.0
CHC C:HEM200 3.4 68.7 1.0
CG C:HIS99 4.1 81.2 1.0
ND1 C:HIS99 4.2 79.3 1.0
C3A C:HEM200 4.3 70.0 1.0
C2A C:HEM200 4.3 70.8 1.0
C3D C:HEM200 4.3 72.6 1.0
C2C C:HEM200 4.3 69.2 1.0
C2B C:HEM200 4.3 68.5 1.0
C3B C:HEM200 4.3 68.4 1.0
C2D C:HEM200 4.3 71.4 1.0
C3C C:HEM200 4.3 70.2 1.0
CG2 C:VAL71 4.7 60.2 1.0
CE1 C:HIS67 4.9 63.6 1.0

Iron binding site 4 out of 8 in 3wcv

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

b:54.7
occ:1.00
FE D:HEM201 0.0 54.7 1.0
O1 D:OXY202 1.8 58.0 1.0
NA D:HEM201 2.0 57.1 1.0
NC D:HEM201 2.0 59.9 1.0
NB D:HEM201 2.0 58.8 1.0
ND D:HEM201 2.0 60.4 1.0
NE2 D:HIS99 2.1 56.5 1.0
O2 D:OXY202 2.7 64.5 1.0
CE1 D:HIS99 2.9 58.5 1.0
C1D D:HEM201 3.0 60.5 1.0
C4C D:HEM201 3.0 60.0 1.0
C1C D:HEM201 3.0 60.6 1.0
C1B D:HEM201 3.0 55.9 1.0
C4A D:HEM201 3.0 55.8 1.0
C4D D:HEM201 3.0 59.8 1.0
C1A D:HEM201 3.1 55.1 1.0
C4B D:HEM201 3.1 59.0 1.0
CD2 D:HIS99 3.2 60.5 1.0
CHB D:HEM201 3.4 55.4 1.0
CHD D:HEM201 3.4 60.9 1.0
CHA D:HEM201 3.4 57.0 1.0
CHC D:HEM201 3.4 60.9 1.0
ND1 D:HIS99 4.1 61.2 1.0
CG D:HIS99 4.2 63.6 1.0
C3A D:HEM201 4.3 55.2 1.0
C2A D:HEM201 4.3 54.3 1.0
C2C D:HEM201 4.3 60.0 1.0
C3D D:HEM201 4.3 60.6 1.0
C2B D:HEM201 4.3 57.1 1.0
C3B D:HEM201 4.3 58.7 1.0
C2D D:HEM201 4.3 60.6 1.0
C3C D:HEM201 4.3 60.4 1.0
CG2 D:VAL71 4.5 44.3 1.0
CE1 D:HIS67 4.9 42.2 1.0

Iron binding site 5 out of 8 in 3wcv

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

b:53.4
occ:1.00
FE E:HEM200 0.0 53.4 1.0
O1 E:OXY201 1.8 54.3 1.0
NA E:HEM200 2.0 46.7 1.0
NC E:HEM200 2.0 46.8 1.0
ND E:HEM200 2.0 48.0 1.0
NB E:HEM200 2.0 47.4 1.0
NE2 E:HIS94 2.1 53.2 1.0
O2 E:OXY201 2.8 61.0 1.0
C1D E:HEM200 3.0 48.3 1.0
C4C E:HEM200 3.0 47.9 1.0
C4D E:HEM200 3.0 48.3 1.0
C1C E:HEM200 3.0 46.8 1.0
C1A E:HEM200 3.0 47.7 1.0
C1B E:HEM200 3.0 48.5 1.0
C4A E:HEM200 3.0 47.8 1.0
C4B E:HEM200 3.1 46.8 1.0
CD2 E:HIS94 3.1 56.4 1.0
CE1 E:HIS94 3.1 55.5 1.0
CHD E:HEM200 3.4 48.1 1.0
CHA E:HEM200 3.4 48.8 1.0
CHB E:HEM200 3.4 48.1 1.0
CHC E:HEM200 3.4 46.9 1.0
ND1 E:HIS94 4.2 55.7 1.0
C2A E:HEM200 4.2 49.5 1.0
C3A E:HEM200 4.3 49.3 1.0
CG E:HIS94 4.3 58.2 1.0
C3D E:HEM200 4.3 49.6 1.0
C2C E:HEM200 4.3 48.1 1.0
C2D E:HEM200 4.3 49.0 1.0
C2B E:HEM200 4.3 49.8 1.0
C3B E:HEM200 4.3 48.8 1.0
C3C E:HEM200 4.3 49.4 1.0
CG2 E:VAL66 4.6 42.3 1.0
CE1 E:HIS62 4.8 39.1 1.0

Iron binding site 6 out of 8 in 3wcv

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

b:60.4
occ:1.00
FE F:HEM201 0.0 60.4 1.0
O1 F:OXY202 1.8 66.8 1.0
NC F:HEM201 2.0 56.3 1.0
NB F:HEM201 2.0 55.8 1.0
NA F:HEM201 2.0 56.7 1.0
ND F:HEM201 2.0 58.4 1.0
NE2 F:HIS95 2.1 72.5 1.0
O2 F:OXY202 2.8 67.5 1.0
C1D F:HEM201 3.0 58.4 1.0
C4C F:HEM201 3.0 57.8 1.0
C1B F:HEM201 3.0 56.3 1.0
C4D F:HEM201 3.0 58.0 1.0
C1C F:HEM201 3.0 56.7 1.0
CE1 F:HIS95 3.1 76.8 1.0
C1A F:HEM201 3.1 56.1 1.0
C4A F:HEM201 3.1 55.5 1.0
C4B F:HEM201 3.1 58.2 1.0
CD2 F:HIS95 3.1 77.6 1.0
CHD F:HEM201 3.4 58.1 1.0
CHB F:HEM201 3.4 55.3 1.0
CHA F:HEM201 3.4 57.0 1.0
CHC F:HEM201 3.4 58.5 1.0
ND1 F:HIS95 4.2 78.2 1.0
CG F:HIS95 4.3 78.5 1.0
C3A F:HEM201 4.3 53.7 1.0
C2A F:HEM201 4.3 56.0 1.0
C2C F:HEM201 4.3 56.4 1.0
C3D F:HEM201 4.3 58.0 1.0
C3B F:HEM201 4.3 58.9 1.0
C2B F:HEM201 4.3 59.2 1.0
C2D F:HEM201 4.3 57.8 1.0
C3C F:HEM201 4.3 58.0 1.0
CG2 F:VAL67 4.7 44.7 1.0
CE1 F:HIS63 4.8 46.6 1.0

Iron binding site 7 out of 8 in 3wcv

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

b:66.8
occ:1.00
FE G:HEM200 0.0 66.8 1.0
O1 G:OXY201 1.8 70.2 1.0
NC G:HEM200 2.0 67.5 1.0
NB G:HEM200 2.0 68.0 1.0
NA G:HEM200 2.0 69.3 1.0
ND G:HEM200 2.0 68.9 1.0
NE2 G:HIS99 2.1 75.3 1.0
O2 G:OXY201 2.8 70.6 1.0
CE1 G:HIS99 3.0 77.3 1.0
C4C G:HEM200 3.0 68.2 1.0
C1C G:HEM200 3.0 67.9 1.0
C1D G:HEM200 3.0 67.9 1.0
C1B G:HEM200 3.0 66.8 1.0
C4D G:HEM200 3.0 68.8 1.0
C4A G:HEM200 3.0 68.9 1.0
C1A G:HEM200 3.1 69.9 1.0
C4B G:HEM200 3.1 69.0 1.0
CD2 G:HIS99 3.1 78.8 1.0
CHB G:HEM200 3.4 66.3 1.0
CHD G:HEM200 3.4 68.3 1.0
CHA G:HEM200 3.4 69.8 1.0
CHC G:HEM200 3.4 68.8 1.0
ND1 G:HIS99 4.1 78.8 1.0
CG G:HIS99 4.1 79.8 1.0
C3A G:HEM200 4.3 70.9 1.0
C2A G:HEM200 4.3 70.6 1.0
C2C G:HEM200 4.3 67.9 1.0
C3B G:HEM200 4.3 68.4 1.0
C2B G:HEM200 4.3 68.0 1.0
C3D G:HEM200 4.3 68.9 1.0
C2D G:HEM200 4.3 68.0 1.0
C3C G:HEM200 4.3 67.9 1.0
CE1 G:HIS67 4.7 46.9 1.0
CG2 G:VAL71 4.8 62.1 1.0

Iron binding site 8 out of 8 in 3wcv

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

b:57.1
occ:1.00
FE H:HEM201 0.0 57.1 1.0
O1 H:OXY202 1.8 65.2 1.0
ND H:HEM201 2.0 55.3 1.0
NA H:HEM201 2.0 54.3 1.0
NC H:HEM201 2.0 53.4 1.0
NB H:HEM201 2.0 53.7 1.0
NE2 H:HIS99 2.1 57.5 1.0
O2 H:OXY202 2.8 71.5 1.0
C1D H:HEM201 3.0 54.8 1.0
C4C H:HEM201 3.0 52.5 1.0
C4D H:HEM201 3.0 57.8 1.0
C1C H:HEM201 3.0 52.6 1.0
C1B H:HEM201 3.0 52.9 1.0
CE1 H:HIS99 3.1 58.3 1.0
C4A H:HEM201 3.1 53.2 1.0
C1A H:HEM201 3.1 55.4 1.0
C4B H:HEM201 3.1 54.5 1.0
CD2 H:HIS99 3.1 60.6 1.0
CHD H:HEM201 3.4 53.1 1.0
CHB H:HEM201 3.4 53.8 1.0
CHA H:HEM201 3.4 57.2 1.0
CHC H:HEM201 3.4 54.3 1.0
ND1 H:HIS99 4.2 59.5 1.0
CG H:HIS99 4.2 62.0 1.0
C3A H:HEM201 4.3 54.1 1.0
C2A H:HEM201 4.3 55.3 1.0
C2C H:HEM201 4.3 53.0 1.0
C3D H:HEM201 4.3 57.8 1.0
C2D H:HEM201 4.3 57.1 1.0
C2B H:HEM201 4.3 54.3 1.0
C3B H:HEM201 4.3 55.7 1.0
C3C H:HEM201 4.3 53.7 1.0
CG2 H:VAL71 4.7 41.2 1.0
CG1 H:VAL71 4.9 39.5 1.0
CE1 H:HIS67 4.9 42.7 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 22:35:25 2024

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