Magnesium 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

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

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:

Iron

(Fe)

2 atoms

The binding sites of Magnesium 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 Magnesium atom.
In total 2 binding sites of Magnesium 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 Magnesium binding site number: 1; 2;

Magnesium 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 Magnesium with other atoms in the Mg 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 B:Mg147 b:9.1 occ:1.00 MG B:HEG147 0.0 9.1 1.0 NB B:HEG147 2.0 9.8 1.0 NC B:HEG147 2.0 8.8 1.0 ND B:HEG147 2.0 10.2 1.0 NA B:HEG147 2.0 10.9 1.0 NE2 B:HIS92 2.2 12.5 1.0 CE1 B:HIS92 3.0 13.8 1.0 C4B B:HEG147 3.0 9.7 1.0 C1D B:HEG147 3.0 10.0 1.0 C1B B:HEG147 3.1 9.8 1.0 C4A B:HEG147 3.1 11.7 1.0 C4C B:HEG147 3.1 8.4 1.0 C1A B:HEG147 3.1 12.1 1.0 C4D B:HEG147 3.1 10.7 1.0 C1C B:HEG147 3.1 8.7 1.0 CD2 B:HIS92 3.3 12.6 1.0 CHD B:HEG147 3.4 8.9 1.0 CHB B:HEG147 3.4 11.1 1.0 CHC B:HEG147 3.5 9.2 1.0 CHA B:HEG147 3.5 11.3 1.0 CG2 B:VAL67 4.1 14.0 1.0 ND1 B:HIS92 4.2 12.6 1.0 NE2 B:HIS63 4.2 15.1 1.0 C3B B:HEG147 4.3 10.7 1.0 C2D B:HEG147 4.3 10.2 1.0 C2A B:HEG147 4.3 12.5 1.0 C2B B:HEG147 4.3 9.9 1.0 C3A B:HEG147 4.3 12.2 1.0 C3C B:HEG147 4.3 8.6 1.0 C3D B:HEG147 4.3 11.4 1.0 C2C B:HEG147 4.3 8.5 1.0 CG B:HIS92 4.3 12.1 1.0 CE1 B:HIS63 4.5 15.6 1.0

Magnesium 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 Magnesium with other atoms in the Mg 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 D:Mg147 b:12.1 occ:1.00 MG D:HEG147 0.0 12.1 1.0 ND D:HEG147 2.0 12.6 1.0 NC D:HEG147 2.0 10.9 1.0 NB D:HEG147 2.0 12.3 1.0 NA D:HEG147 2.1 12.7 1.0 NE2 D:HIS92 2.2 11.3 1.0 CE1 D:HIS92 3.1 12.7 1.0 C4B D:HEG147 3.1 12.1 1.0 C1A D:HEG147 3.1 13.2 1.0 C1B D:HEG147 3.1 11.6 1.0 C1D D:HEG147 3.1 13.2 1.0 C1C D:HEG147 3.1 10.9 1.0 C4A D:HEG147 3.1 12.8 1.0 C4C D:HEG147 3.1 11.5 1.0 C4D D:HEG147 3.1 12.9 1.0 CD2 D:HIS92 3.4 12.5 1.0 CHA D:HEG147 3.4 12.2 1.0 CHC D:HEG147 3.4 11.6 1.0 CHB D:HEG147 3.5 12.1 1.0 CHD D:HEG147 3.5 12.1 1.0 CG2 D:VAL67 4.2 13.0 1.0 ND1 D:HIS92 4.3 12.8 1.0 C2A D:HEG147 4.3 14.6 1.0 C3B D:HEG147 4.3 12.6 1.0 C3D D:HEG147 4.3 14.1 1.0 C2D D:HEG147 4.3 13.2 1.0 C2B D:HEG147 4.3 12.2 1.0 NE2 D:HIS63 4.3 14.9 1.0 C3A D:HEG147 4.3 13.2 1.0 C3C D:HEG147 4.3 10.9 1.0 C2C D:HEG147 4.3 11.0 1.0 CG D:HIS92 4.4 12.2 1.0 CE1 D:HIS63 4.7 16.0 1.0 CD1 D:LEU96 5.0 12.1 1.0

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