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Iron in PDB 3zs1: Human Myeloperoxidase Inactivated By TX5

Enzymatic activity of Human Myeloperoxidase Inactivated By TX5

All present enzymatic activity of Human Myeloperoxidase Inactivated By TX5:
1.11.2.2;

Protein crystallography data

The structure of Human Myeloperoxidase Inactivated By TX5, PDB code: 3zs1 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) 110.43 / 2.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 93.130, 63.790, 111.350, 90.00, 97.32, 90.00
R / Rfree (%) 18.7 / 24.4

Other elements in 3zs1:

The structure of Human Myeloperoxidase Inactivated By TX5 also contains other interesting chemical elements:

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

Iron Binding Sites:

The binding sites of Iron atom in the Human Myeloperoxidase Inactivated By TX5 (pdb code 3zs1). 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 TX5, PDB code: 3zs1:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 3zs1

Go back to Iron Binding Sites List in 3zs1
Iron binding site 1 out of 2 in the Human Myeloperoxidase Inactivated By TX5


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 TX5 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe605

b:2.7
occ:1.00
FE A:HEM605 0.0 2.7 1.0
ND A:HEM605 2.1 2.0 1.0
NB A:HEM605 2.1 3.3 1.0
NC A:HEM605 2.1 2.3 1.0
NA A:HEM605 2.1 3.0 1.0
NE2 C:HIS336 2.3 4.0 1.0
O A:HOH2040 2.7 2.0 1.0
C1D A:HEM605 3.0 2.0 1.0
C1B A:HEM605 3.0 2.7 1.0
C4C A:HEM605 3.1 2.0 1.0
C4D A:HEM605 3.1 2.0 1.0
C4B A:HEM605 3.1 2.8 1.0
C4A A:HEM605 3.1 3.4 1.0
C1A A:HEM605 3.1 2.7 1.0
C1C A:HEM605 3.1 2.0 1.0
CE1 C:HIS336 3.2 4.6 1.0
CD2 C:HIS336 3.3 4.1 1.0
CHD A:HEM605 3.4 2.0 1.0
CHB A:HEM605 3.4 3.6 1.0
CHA A:HEM605 3.4 2.1 1.0
CHC A:HEM605 3.4 2.0 1.0
C3A A:HEM605 4.3 3.1 1.0
C2A A:HEM605 4.3 3.1 1.0
C3C A:HEM605 4.3 2.0 1.0
C3D A:HEM605 4.3 2.0 1.0
C3B A:HEM605 4.3 3.6 1.0
C2D A:HEM605 4.3 2.0 1.0
C2B A:HEM605 4.3 2.8 1.0
ND1 C:HIS336 4.4 4.2 1.0
C2C A:HEM605 4.4 2.0 1.0
CG C:HIS336 4.4 3.6 1.0
CD2 C:LEU417 4.7 2.0 1.0
NE2 A:GLN91 4.9 2.6 1.0
CG A:GLN91 5.0 4.8 1.0
O C:HOH2044 5.0 7.7 1.0

Iron binding site 2 out of 2 in 3zs1

Go back to Iron Binding Sites List in 3zs1
Iron binding site 2 out of 2 in the Human Myeloperoxidase Inactivated By TX5


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 TX5 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe605

b:9.2
occ:1.00
FE B:HEM605 0.0 9.2 1.0
ND B:HEM605 2.1 9.5 1.0
NB B:HEM605 2.1 10.5 1.0
NC B:HEM605 2.1 9.0 1.0
NA B:HEM605 2.1 9.2 1.0
NE2 D:HIS336 2.3 11.3 1.0
O B:HOH2038 2.9 2.0 1.0
C4D B:HEM605 3.0 9.2 1.0
C4B B:HEM605 3.1 9.6 1.0
C1D B:HEM605 3.1 9.1 1.0
C1B B:HEM605 3.1 10.3 1.0
C1C B:HEM605 3.1 9.3 1.0
C1A B:HEM605 3.1 9.1 1.0
C4C B:HEM605 3.1 9.1 1.0
C4A B:HEM605 3.1 8.8 1.0
CD2 D:HIS336 3.2 11.0 1.0
CE1 D:HIS336 3.3 10.8 1.0
CHC B:HEM605 3.4 9.1 1.0
CHA B:HEM605 3.4 9.7 1.0
CHD B:HEM605 3.4 8.8 1.0
CHB B:HEM605 3.5 9.7 1.0
C3A B:HEM605 4.3 8.5 1.0
C2A B:HEM605 4.3 8.7 1.0
C3D B:HEM605 4.3 8.3 1.0
C3B B:HEM605 4.3 11.2 1.0
C2D B:HEM605 4.3 8.6 1.0
C3C B:HEM605 4.4 8.7 1.0
C2B B:HEM605 4.4 11.0 1.0
C2C B:HEM605 4.4 9.1 1.0
CG D:HIS336 4.4 9.8 1.0
ND1 D:HIS336 4.4 10.2 1.0
NE2 B:GLN91 4.7 7.1 1.0
CD2 D:LEU417 4.9 9.1 1.0
CG B:GLN91 5.0 7.5 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 Aug 4 23:26:04 2024

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