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Iron in PDB 3zs0: Human Myeloperoxidase Inactivated By TX2

Enzymatic activity of Human Myeloperoxidase Inactivated By TX2

All present enzymatic activity of Human Myeloperoxidase Inactivated By TX2:
1.11.2.2;

Protein crystallography data

The structure of Human Myeloperoxidase Inactivated By TX2, PDB code: 3zs0 was solved by A.K.Tiden, T.Sjogren, M.Svensson, A.Bernlind, R.Senthilmohan, F.Auchere, H.Norman, P.O.Markgren, S.Gustavsson, S.Schmidt, S.Lundquist, L.V.Forbes, N.J.Magon, G.N.Jameson, H.Eriksson, A.J.Kettle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 93.905, 64.111, 111.452, 90.00, 97.12, 90.00
R / Rfree (%) 17 / 20.7

Other elements in 3zs0:

The structure of Human Myeloperoxidase Inactivated By TX2 also contains other interesting chemical elements:

Fluorine (F) 2 atoms
Calcium (Ca) 2 atoms
Chlorine (Cl) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Human Myeloperoxidase Inactivated By TX2 (pdb code 3zs0). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Human Myeloperoxidase Inactivated By TX2, PDB code: 3zs0:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 3zs0

Go back to Iron Binding Sites List in 3zs0
Iron binding site 1 out of 2 in the Human Myeloperoxidase Inactivated By TX2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Human Myeloperoxidase Inactivated By TX2 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe1580

b:14.0
occ:1.00
FE C:HEM1580 0.0 14.0 1.0
NC C:HEM1580 2.1 11.4 1.0
ND C:HEM1580 2.1 12.8 1.0
NE2 C:HIS336 2.1 12.8 1.0
NB C:HEM1580 2.1 15.3 1.0
NA C:HEM1580 2.1 15.0 1.0
O A:HOH2090 2.9 16.0 1.0
C4C C:HEM1580 3.1 11.4 1.0
C1D C:HEM1580 3.1 12.2 1.0
CE1 C:HIS336 3.1 13.9 1.0
C4B C:HEM1580 3.1 15.1 1.0
C1C C:HEM1580 3.1 11.0 1.0
C4D C:HEM1580 3.1 13.2 1.0
CD2 C:HIS336 3.1 12.1 1.0
C4A C:HEM1580 3.1 15.6 1.0
C1A C:HEM1580 3.1 15.3 1.0
C1B C:HEM1580 3.2 16.6 1.0
CHD C:HEM1580 3.4 10.3 1.0
CHC C:HEM1580 3.4 11.9 1.0
CHA C:HEM1580 3.5 14.7 1.0
CHB C:HEM1580 3.5 16.0 1.0
ND1 C:HIS336 4.2 12.9 1.0
CG C:HIS336 4.3 12.3 1.0
C3C C:HEM1580 4.3 10.1 1.0
C2D C:HEM1580 4.4 12.2 1.0
C3A C:HEM1580 4.4 15.0 1.0
C3B C:HEM1580 4.4 17.8 1.0
C2A C:HEM1580 4.4 14.9 1.0
C2C C:HEM1580 4.4 10.7 1.0
C3D C:HEM1580 4.4 12.1 1.0
C2B C:HEM1580 4.5 17.1 1.0
CD2 C:LEU417 4.7 8.4 1.0
O C:HOH2086 4.9 15.2 1.0

Iron binding site 2 out of 2 in 3zs0

Go back to Iron Binding Sites List in 3zs0
Iron binding site 2 out of 2 in the Human Myeloperoxidase Inactivated By TX2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Human Myeloperoxidase Inactivated By TX2 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe1580

b:17.6
occ:1.00
FE D:HEM1580 0.0 17.6 1.0
NA D:HEM1580 2.1 18.3 1.0
NB D:HEM1580 2.1 18.8 1.0
NC D:HEM1580 2.1 15.7 1.0
ND D:HEM1580 2.1 16.6 1.0
NE2 D:HIS336 2.1 17.0 1.0
O B:HOH2079 2.9 29.4 1.0
CE1 D:HIS336 3.1 16.5 1.0
C4A D:HEM1580 3.1 18.7 1.0
C1B D:HEM1580 3.1 20.6 1.0
C4D D:HEM1580 3.1 17.3 1.0
C1A D:HEM1580 3.1 18.5 1.0
C4B D:HEM1580 3.1 18.9 1.0
C1C D:HEM1580 3.1 16.6 1.0
C4C D:HEM1580 3.1 15.3 1.0
C1D D:HEM1580 3.1 15.5 1.0
CD2 D:HIS336 3.2 14.9 1.0
CHA D:HEM1580 3.4 18.4 1.0
CHB D:HEM1580 3.4 19.6 1.0
CHC D:HEM1580 3.5 17.6 1.0
CHD D:HEM1580 3.5 14.9 1.0
ND1 D:HIS336 4.2 14.2 1.0
CG D:HIS336 4.3 14.9 1.0
C3A D:HEM1580 4.3 18.5 1.0
C2A D:HEM1580 4.3 18.4 1.0
C3B D:HEM1580 4.4 21.5 1.0
C3D D:HEM1580 4.4 17.7 1.0
C3C D:HEM1580 4.4 14.6 1.0
C2B D:HEM1580 4.4 22.0 1.0
C2D D:HEM1580 4.4 16.3 1.0
C2C D:HEM1580 4.4 15.4 1.0
CD2 D:LEU417 4.7 15.5 1.0
O D:HOH2060 4.7 29.3 1.0
NE2 B:GLN91 5.0 17.8 1.0

Reference:

A.K.Tiden, T.Sjogren, M.Svensson, A.Bernlind, R.Senthilmohan, F.Auchere, H.Norman, P.O.Markgren, S.Gustavsson, S.Schmidt, S.Lundquist, L.V.Forbes, N.J.Magon, L.N.Paton, G.N.Jameson, H.Eriksson, A.J.Kettle. 2-Thioxanthines Are Mechanism-Based Inactivators of Myeloperoxidase That Block Oxidative Stress During Inflammation. J.Biol.Chem. V. 286 37578 2011.
ISSN: ISSN 0021-9258
PubMed: 21880720
DOI: 10.1074/JBC.M111.266981
Page generated: Sun Dec 13 15:27:30 2020

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