Atomistry » Iron » PDB 1qov-1ra5 » 1qsi
Atomistry »
  Iron »
    PDB 1qov-1ra5 »
      1qsi »

Iron in PDB 1qsi: 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: 1qsi 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 1qsi:

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 1qsi). 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: 1qsi:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1qsi

Go back to Iron Binding Sites List in 1qsi
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:11.2
occ:1.00
FE A:HEM142 0.0 11.2 1.0
C A:CMO143 1.8 10.4 1.0
NA A:HEM142 2.0 11.6 1.0
NB A:HEM142 2.0 10.8 1.0
ND A:HEM142 2.0 11.8 1.0
NC A:HEM142 2.0 11.1 1.0
NE2 A:HIS87 2.2 12.0 1.0
O A:CMO143 3.0 14.9 1.0
C1D A:HEM142 3.0 11.3 1.0
C4D A:HEM142 3.0 13.6 1.0
C1A A:HEM142 3.1 13.3 1.0
C4B A:HEM142 3.1 10.7 1.0
C1B A:HEM142 3.1 12.0 1.0
C4A A:HEM142 3.1 13.3 1.0
C4C A:HEM142 3.1 11.4 1.0
C1C A:HEM142 3.1 11.2 1.0
CE1 A:HIS87 3.1 10.9 1.0
CD2 A:HIS87 3.3 11.2 1.0
CHA A:HEM142 3.4 12.4 1.0
CHC A:HEM142 3.4 11.2 1.0
CHD A:HEM142 3.4 12.0 1.0
CHB A:HEM142 3.5 12.3 1.0
C3D A:HEM142 4.2 12.9 1.0
C2A A:HEM142 4.3 14.2 1.0
C3B A:HEM142 4.3 11.4 1.0
ND1 A:HIS87 4.3 11.7 1.0
C2C A:HEM142 4.3 10.9 1.0
C3A A:HEM142 4.3 13.8 1.0
C2B A:HEM142 4.3 11.1 1.0
C2D A:HEM142 4.3 13.4 1.0
C3C A:HEM142 4.3 10.9 1.0
CG A:HIS87 4.4 11.7 1.0
NE2 A:HIS58 4.4 15.8 1.0
CD1 A:LEU91 4.9 12.7 1.0

Iron binding site 2 out of 2 in 1qsi

Go back to Iron Binding Sites List in 1qsi
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:8.4
occ:1.00
FE C:HEM142 0.0 8.4 1.0
C C:CMO143 1.8 13.7 1.0
NC C:HEM142 2.0 8.7 1.0
NA C:HEM142 2.0 10.8 1.0
ND C:HEM142 2.0 8.3 1.0
NB C:HEM142 2.1 8.4 1.0
NE2 C:HIS87 2.2 6.3 1.0
O C:CMO143 2.9 14.5 1.0
C1D C:HEM142 3.0 8.2 1.0
C1C C:HEM142 3.0 8.5 1.0
C4D C:HEM142 3.0 8.0 1.0
C4C C:HEM142 3.0 8.6 1.0
C1A C:HEM142 3.0 11.0 1.0
C4B C:HEM142 3.1 8.9 1.0
CE1 C:HIS87 3.1 7.0 1.0
C4A C:HEM142 3.1 11.0 1.0
C1B C:HEM142 3.1 8.5 1.0
CD2 C:HIS87 3.3 7.7 1.0
CHA C:HEM142 3.4 10.0 1.0
CHC C:HEM142 3.4 9.0 1.0
CHD C:HEM142 3.4 8.3 1.0
CHB C:HEM142 3.5 9.9 1.0
C2C C:HEM142 4.2 9.1 1.0
C3D C:HEM142 4.2 9.4 1.0
C2D C:HEM142 4.3 8.2 1.0
ND1 C:HIS87 4.3 9.0 1.0
C2A C:HEM142 4.3 12.2 1.0
C3C C:HEM142 4.3 8.9 1.0
C3A C:HEM142 4.3 12.1 1.0
C3B C:HEM142 4.3 10.1 1.0
C2B C:HEM142 4.3 9.3 1.0
CG C:HIS87 4.3 7.1 1.0
NE2 C:HIS58 4.5 12.8 1.0
CG2 C:VAL62 4.9 9.2 1.0
CD1 C:LEU91 4.9 12.9 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

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy