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Iron in PDB 1qsh: Magnesium(II)-and Zinc(II)-Protoporphyrin IX'S Stabilize the Lowest Oxygen Affinity State of Human Hemoglobin Even More Strongly Than Deoxyheme

Protein crystallography data

The structure of Magnesium(II)-and Zinc(II)-Protoporphyrin IX'S Stabilize the Lowest Oxygen Affinity State of Human Hemoglobin Even More Strongly Than Deoxyheme, PDB code: 1qsh was solved by G.Miyazaki, H.Morimoto, K.-M.Yun, S.-Y.Park, A.Nakagawa, H.Minagawa, N.Shibayama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 63.150, 83.590, 53.800, 90.00, 99.34, 90.00
R / Rfree (%) n/a / n/a

Other elements in 1qsh:

The structure of Magnesium(II)-and Zinc(II)-Protoporphyrin IX'S Stabilize the Lowest Oxygen Affinity State of Human Hemoglobin Even More Strongly Than Deoxyheme also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Magnesium(II)-and Zinc(II)-Protoporphyrin IX'S Stabilize the Lowest Oxygen Affinity State of Human Hemoglobin Even More Strongly Than Deoxyheme (pdb code 1qsh). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Magnesium(II)-and Zinc(II)-Protoporphyrin IX'S Stabilize the Lowest Oxygen Affinity State of Human Hemoglobin Even More Strongly Than Deoxyheme, PDB code: 1qsh:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1qsh

Go back to Iron Binding Sites List in 1qsh
Iron binding site 1 out of 2 in the Magnesium(II)-and Zinc(II)-Protoporphyrin IX'S Stabilize the Lowest Oxygen Affinity State of Human Hemoglobin Even More Strongly Than Deoxyheme


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Magnesium(II)-and Zinc(II)-Protoporphyrin IX'S Stabilize the Lowest Oxygen Affinity State of Human Hemoglobin Even More Strongly Than Deoxyheme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe142

b:10.9
occ:1.00
FE A:HEM142 0.0 10.9 1.0
NB A:HEM142 2.0 10.1 1.0
ND A:HEM142 2.0 11.0 1.0
NC A:HEM142 2.0 10.7 1.0
NA A:HEM142 2.1 12.3 1.0
NE2 A:HIS87 2.3 12.0 1.0
C4B A:HEM142 3.1 10.8 1.0
C1D A:HEM142 3.1 9.8 1.0
C4D A:HEM142 3.1 10.7 1.0
C1A A:HEM142 3.1 13.0 1.0
C4C A:HEM142 3.1 10.1 1.0
C1C A:HEM142 3.1 11.2 1.0
C1B A:HEM142 3.1 10.9 1.0
C4A A:HEM142 3.1 13.2 1.0
CE1 A:HIS87 3.2 11.4 1.0
CD2 A:HIS87 3.4 12.1 1.0
CHD A:HEM142 3.4 10.2 1.0
CHB A:HEM142 3.5 11.4 1.0
CHA A:HEM142 3.5 11.0 1.0
CHC A:HEM142 3.5 11.4 1.0
O A:HOH151 3.6 19.3 1.0
C3D A:HEM142 4.3 10.6 1.0
C2B A:HEM142 4.3 11.5 1.0
C2D A:HEM142 4.3 10.2 1.0
C3B A:HEM142 4.3 11.1 1.0
ND1 A:HIS87 4.3 12.9 1.0
C2C A:HEM142 4.3 10.7 1.0
C3C A:HEM142 4.3 10.1 1.0
C3A A:HEM142 4.3 14.0 1.0
C2A A:HEM142 4.3 14.3 1.0
CE1 A:HIS58 4.4 14.3 1.0
NE2 A:HIS58 4.4 13.9 1.0
CG A:HIS87 4.5 12.1 1.0
CD1 A:LEU91 4.5 13.9 1.0

Iron binding site 2 out of 2 in 1qsh

Go back to Iron Binding Sites List in 1qsh
Iron binding site 2 out of 2 in the Magnesium(II)-and Zinc(II)-Protoporphyrin IX'S Stabilize the Lowest Oxygen Affinity State of Human Hemoglobin Even More Strongly Than Deoxyheme


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Magnesium(II)-and Zinc(II)-Protoporphyrin IX'S Stabilize the Lowest Oxygen Affinity State of Human Hemoglobin Even More Strongly Than Deoxyheme within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe142

b:9.4
occ:1.00
FE C:HEM142 0.0 9.4 1.0
NB C:HEM142 2.0 10.0 1.0
ND C:HEM142 2.0 9.0 1.0
NC C:HEM142 2.1 9.2 1.0
NA C:HEM142 2.1 11.2 1.0
NE2 C:HIS87 2.3 8.4 1.0
C4B C:HEM142 3.0 9.4 1.0
C1D C:HEM142 3.1 9.0 1.0
C1B C:HEM142 3.1 10.2 1.0
C1C C:HEM142 3.1 8.5 1.0
C4D C:HEM142 3.1 9.2 1.0
C4A C:HEM142 3.1 10.9 1.0
C4C C:HEM142 3.1 9.0 1.0
C1A C:HEM142 3.1 11.4 1.0
CE1 C:HIS87 3.1 8.8 1.0
CD2 C:HIS87 3.3 8.8 1.0
CHC C:HEM142 3.4 9.0 1.0
CHB C:HEM142 3.4 11.4 1.0
CHA C:HEM142 3.5 10.3 1.0
CHD C:HEM142 3.5 8.8 1.0
O C:HOH164 3.6 21.2 1.0
C2B C:HEM142 4.3 10.1 1.0
C3B C:HEM142 4.3 9.2 1.0
C3D C:HEM142 4.3 10.8 1.0
C2D C:HEM142 4.3 9.8 1.0
C2C C:HEM142 4.3 7.9 1.0
ND1 C:HIS87 4.3 9.7 1.0
C2A C:HEM142 4.3 12.5 1.0
C3A C:HEM142 4.4 11.7 1.0
NE2 C:HIS58 4.4 14.8 1.0
C3C C:HEM142 4.4 8.7 1.0
CG C:HIS87 4.4 8.4 1.0
CE1 C:HIS58 4.5 14.7 1.0
CD1 C:LEU91 4.5 10.9 1.0

Reference:

G.Miyazaki, H.Morimoto, K.M.Yun, S.Y.Park, A.Nakagawa, H.Minagawa, N.Shibayama. Magnesium(II) and Zinc(II)-Protoporphyrin IX'S Stabilize the Lowest Oxygen Affinity State of Human Hemoglobin Even More Strongly Than Deoxyheme. J.Mol.Biol. V. 292 1121 1999.
ISSN: ISSN 0022-2836
PubMed: 10512707
DOI: 10.1006/JMBI.1999.3124
Page generated: Sat Aug 3 13:52:59 2024

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