Atomistry » Iron » PDB 7o4j-7oqr » 7oih
Atomistry »
  Iron »
    PDB 7o4j-7oqr »
      7oih »

Iron in PDB 7oih: Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase

Enzymatic activity of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase

All present enzymatic activity of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase:
1.11.2.2;

Protein crystallography data

The structure of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase, PDB code: 7oih was solved by L.Krawczyk, S.Semwal, J.Bouckaert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.99 / 2.60
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 155.91, 144.634, 236.454, 90, 91.53, 90
R / Rfree (%) 17.9 / 22

Other elements in 7oih:

The structure of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase also contains other interesting chemical elements:

Chlorine (Cl) 36 atoms
Calcium (Ca) 8 atoms
Fluorine (F) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase (pdb code 7oih). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase, PDB code: 7oih:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Iron binding site 1 out of 8 in 7oih

Go back to Iron Binding Sites List in 7oih
Iron binding site 1 out of 8 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe805

b:46.1
occ:1.00
FE A:HEM805 0.0 46.1 1.0
ND A:HEM805 1.9 52.3 1.0
NA A:HEM805 2.0 50.1 1.0
NE2 A:HIS502 2.1 44.0 1.0
O A:HOH905 2.1 48.4 1.0
NC A:HEM805 2.1 48.5 1.0
NB A:HEM805 2.1 54.5 1.0
C4D A:HEM805 2.9 50.5 1.0
C1D A:HEM805 3.0 43.0 1.0
C1A A:HEM805 3.0 51.3 1.0
C4A A:HEM805 3.0 51.2 1.0
C4C A:HEM805 3.1 43.0 1.0
C1B A:HEM805 3.1 51.1 1.0
CD2 A:HIS502 3.1 40.8 1.0
CE1 A:HIS502 3.1 36.8 1.0
C1C A:HEM805 3.2 50.0 1.0
C4B A:HEM805 3.2 54.8 1.0
CHA A:HEM805 3.3 52.4 1.0
CHD A:HEM805 3.4 41.6 1.0
CHB A:HEM805 3.4 51.5 1.0
CHC A:HEM805 3.5 50.6 1.0
C3A A:HEM805 4.2 53.3 1.0
C2A A:HEM805 4.2 49.5 1.0
C2D A:HEM805 4.2 40.1 1.0
C3D A:HEM805 4.2 43.0 1.0
CG A:HIS502 4.2 35.0 1.0
ND1 A:HIS502 4.2 31.6 1.0
C3C A:HEM805 4.3 44.5 1.0
C2C A:HEM805 4.3 45.0 1.0
C2B A:HEM805 4.3 53.5 1.0
C3B A:HEM805 4.4 57.8 1.0
CD2 A:LEU583 4.5 38.6 1.0
N A:SCN806 4.7 77.1 1.0

Iron binding site 2 out of 8 in 7oih

Go back to Iron Binding Sites List in 7oih
Iron binding site 2 out of 8 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe807

b:51.6
occ:1.00
FE B:HEM807 0.0 51.6 1.0
ND B:HEM807 1.9 54.0 1.0
NE2 B:HIS502 2.0 51.1 1.0
O B:HOH912 2.0 67.0 1.0
NA B:HEM807 2.1 53.6 1.0
NB B:HEM807 2.1 48.3 1.0
NC B:HEM807 2.1 48.1 1.0
C1D B:HEM807 2.9 51.5 1.0
C4D B:HEM807 2.9 47.0 1.0
CD2 B:HIS502 3.0 50.6 1.0
CE1 B:HIS502 3.0 48.9 1.0
C1B B:HEM807 3.1 42.7 1.0
C4B B:HEM807 3.1 51.2 1.0
C1A B:HEM807 3.1 48.2 1.0
C4C B:HEM807 3.1 46.3 1.0
C4A B:HEM807 3.1 47.7 1.0
C1C B:HEM807 3.2 45.7 1.0
CHA B:HEM807 3.4 48.7 1.0
CHD B:HEM807 3.4 43.2 1.0
CHB B:HEM807 3.5 43.6 1.0
CHC B:HEM807 3.5 43.1 1.0
ND1 B:HIS502 4.2 42.6 1.0
C2D B:HEM807 4.2 48.1 1.0
CG B:HIS502 4.2 45.7 1.0
C3D B:HEM807 4.2 44.3 1.0
C3B B:HEM807 4.3 49.9 1.0
C2A B:HEM807 4.3 42.4 1.0
C2B B:HEM807 4.3 49.1 1.0
C3C B:HEM807 4.3 44.5 1.0
C3A B:HEM807 4.3 45.0 1.0
C2C B:HEM807 4.4 43.6 1.0
CD2 B:LEU583 4.6 40.4 1.0
N B:SCN808 4.8 62.9 1.0

Iron binding site 3 out of 8 in 7oih

Go back to Iron Binding Sites List in 7oih
Iron binding site 3 out of 8 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe806

b:54.2
occ:1.00
FE C:HEM806 0.0 54.2 1.0
ND C:HEM806 2.0 59.1 1.0
O C:HOH906 2.0 62.2 1.0
NA C:HEM806 2.0 51.3 1.0
NE2 C:HIS502 2.1 52.1 1.0
NC C:HEM806 2.1 51.2 1.0
NB C:HEM806 2.1 51.2 1.0
C1D C:HEM806 3.0 50.6 1.0
C4D C:HEM806 3.0 48.6 1.0
C4C C:HEM806 3.0 52.3 1.0
C1B C:HEM806 3.0 48.9 1.0
C1A C:HEM806 3.1 49.7 1.0
C4A C:HEM806 3.1 54.2 1.0
CD2 C:HIS502 3.1 50.2 1.0
CE1 C:HIS502 3.1 52.8 1.0
C4B C:HEM806 3.1 51.1 1.0
C1C C:HEM806 3.2 50.2 1.0
CHD C:HEM806 3.4 51.2 1.0
CHA C:HEM806 3.4 46.9 1.0
CHB C:HEM806 3.4 49.4 1.0
CHC C:HEM806 3.5 46.8 1.0
ND1 C:HIS502 4.2 43.0 1.0
C2D C:HEM806 4.2 47.5 1.0
C3C C:HEM806 4.2 45.6 1.0
CG C:HIS502 4.2 45.7 1.0
C3D C:HEM806 4.3 49.8 1.0
C3A C:HEM806 4.3 53.8 1.0
C2C C:HEM806 4.3 44.5 1.0
C2B C:HEM806 4.3 53.3 1.0
C2A C:HEM806 4.3 48.3 1.0
C3B C:HEM806 4.3 52.6 1.0
CD2 C:LEU583 4.6 47.9 1.0
N C:SCN807 4.6 75.6 1.0

Iron binding site 4 out of 8 in 7oih

Go back to Iron Binding Sites List in 7oih
Iron binding site 4 out of 8 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe805

b:53.2
occ:1.00
FE D:HEM805 0.0 53.2 1.0
ND D:HEM805 1.9 51.0 1.0
NA D:HEM805 2.1 53.0 1.0
O D:HOH904 2.1 55.1 1.0
NC D:HEM805 2.1 43.5 1.0
NB D:HEM805 2.1 54.1 1.0
NE2 D:HIS502 2.1 47.3 1.0
C1D D:HEM805 2.9 45.3 1.0
C4D D:HEM805 2.9 48.1 1.0
C4C D:HEM805 3.0 38.5 1.0
C1A D:HEM805 3.0 52.0 1.0
C4B D:HEM805 3.0 52.8 1.0
C1C D:HEM805 3.1 45.0 1.0
C1B D:HEM805 3.1 51.7 1.0
C4A D:HEM805 3.1 50.2 1.0
CE1 D:HIS502 3.1 46.3 1.0
CD2 D:HIS502 3.2 47.0 1.0
CHD D:HEM805 3.3 40.6 1.0
CHA D:HEM805 3.4 53.8 1.0
CHC D:HEM805 3.4 47.8 1.0
CHB D:HEM805 3.5 49.4 1.0
C2D D:HEM805 4.2 45.8 1.0
C3C D:HEM805 4.2 41.1 1.0
C3D D:HEM805 4.2 46.0 1.0
C2C D:HEM805 4.2 43.2 1.0
C2A D:HEM805 4.3 46.4 1.0
N D:SCN806 4.3 53.1 1.0
C3A D:HEM805 4.3 52.9 1.0
ND1 D:HIS502 4.3 37.8 1.0
C3B D:HEM805 4.3 56.2 1.0
CG D:HIS502 4.3 38.8 1.0
C2B D:HEM805 4.3 56.1 1.0
CD2 D:LEU583 4.6 39.6 1.0
O D:HOH944 5.0 49.8 1.0

Iron binding site 5 out of 8 in 7oih

Go back to Iron Binding Sites List in 7oih
Iron binding site 5 out of 8 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe805

b:55.5
occ:1.00
FE E:HEM805 0.0 55.5 1.0
ND E:HEM805 1.9 64.2 1.0
NA E:HEM805 2.0 52.5 1.0
O E:HOH927 2.1 64.1 1.0
NE2 E:HIS502 2.1 56.5 1.0
NC E:HEM805 2.1 54.8 1.0
NB E:HEM805 2.1 54.9 1.0
C4D E:HEM805 2.9 60.4 1.0
C1D E:HEM805 3.0 52.7 1.0
C1A E:HEM805 3.0 51.3 1.0
C4C E:HEM805 3.1 53.1 1.0
C4A E:HEM805 3.1 51.3 1.0
C1B E:HEM805 3.1 53.4 1.0
CD2 E:HIS502 3.1 54.7 1.0
C1C E:HEM805 3.1 54.0 1.0
C4B E:HEM805 3.1 52.5 1.0
CE1 E:HIS502 3.1 55.9 1.0
CHA E:HEM805 3.3 52.5 1.0
CHD E:HEM805 3.4 50.9 1.0
CHB E:HEM805 3.5 55.5 1.0
CHC E:HEM805 3.5 52.0 1.0
C3D E:HEM805 4.2 56.7 1.0
C2D E:HEM805 4.2 52.7 1.0
C2A E:HEM805 4.2 55.6 1.0
ND1 E:HIS502 4.2 51.5 1.0
C3A E:HEM805 4.2 52.2 1.0
CG E:HIS502 4.3 53.5 1.0
C2C E:HEM805 4.3 56.7 1.0
C3C E:HEM805 4.3 56.0 1.0
C2B E:HEM805 4.3 54.1 1.0
C3B E:HEM805 4.4 52.4 1.0
CD2 E:LEU583 4.6 53.0 1.0
N E:SCN806 4.9 64.8 1.0

Iron binding site 6 out of 8 in 7oih

Go back to Iron Binding Sites List in 7oih
Iron binding site 6 out of 8 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe805

b:58.0
occ:1.00
FE F:HEM805 0.0 58.0 1.0
ND F:HEM805 1.9 57.0 1.0
NA F:HEM805 2.0 64.3 1.0
O F:HOH905 2.0 54.3 1.0
NE2 F:HIS502 2.1 50.3 1.0
NB F:HEM805 2.1 61.0 1.0
NC F:HEM805 2.2 57.8 1.0
C4D F:HEM805 2.9 49.5 1.0
C1D F:HEM805 3.0 53.5 1.0
C1A F:HEM805 3.0 54.8 1.0
CD2 F:HIS502 3.1 49.4 1.0
C4B F:HEM805 3.1 60.0 1.0
C1B F:HEM805 3.1 60.5 1.0
C4A F:HEM805 3.1 64.0 1.0
CE1 F:HIS502 3.1 51.2 1.0
C4C F:HEM805 3.1 51.4 1.0
C1C F:HEM805 3.2 57.9 1.0
CHA F:HEM805 3.3 56.6 1.0
CHD F:HEM805 3.4 53.5 1.0
CHB F:HEM805 3.5 61.9 1.0
CHC F:HEM805 3.5 56.0 1.0
C3D F:HEM805 4.2 46.1 1.0
C2D F:HEM805 4.2 44.9 1.0
CG F:HIS502 4.2 44.0 1.0
ND1 F:HIS502 4.2 38.2 1.0
C2A F:HEM805 4.2 50.2 1.0
C3A F:HEM805 4.3 56.3 1.0
C2B F:HEM805 4.3 58.6 1.0
C3B F:HEM805 4.3 58.8 1.0
C3C F:HEM805 4.3 52.5 1.0
C2C F:HEM805 4.3 58.9 1.0
CD2 F:LEU583 4.6 40.8 1.0
N F:SCN806 4.8 71.2 1.0

Iron binding site 7 out of 8 in 7oih

Go back to Iron Binding Sites List in 7oih
Iron binding site 7 out of 8 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Fe806

b:42.3
occ:1.00
FE G:HEM806 0.0 42.3 1.0
ND G:HEM806 1.9 43.5 1.0
NA G:HEM806 2.0 39.3 1.0
NC G:HEM806 2.1 35.7 1.0
O G:HOH917 2.1 54.5 1.0
NE2 G:HIS502 2.1 42.0 1.0
NB G:HEM806 2.1 39.9 1.0
C1D G:HEM806 2.9 40.6 1.0
C4D G:HEM806 3.0 38.1 1.0
C4C G:HEM806 3.0 35.2 1.0
C1A G:HEM806 3.0 35.8 1.0
C1B G:HEM806 3.1 39.2 1.0
C1C G:HEM806 3.1 35.1 1.0
C4A G:HEM806 3.1 40.2 1.0
CE1 G:HIS502 3.1 42.3 1.0
C4B G:HEM806 3.1 39.6 1.0
CD2 G:HIS502 3.1 44.4 1.0
CHA G:HEM806 3.4 37.4 1.0
CHD G:HEM806 3.4 37.6 1.0
CHB G:HEM806 3.5 38.6 1.0
CHC G:HEM806 3.5 32.9 1.0
C3C G:HEM806 4.2 36.1 1.0
C2D G:HEM806 4.2 41.9 1.0
C2C G:HEM806 4.2 39.0 1.0
C3D G:HEM806 4.2 40.7 1.0
C2A G:HEM806 4.2 37.9 1.0
ND1 G:HIS502 4.2 40.2 1.0
C3A G:HEM806 4.3 38.4 1.0
CG G:HIS502 4.3 41.8 1.0
C2B G:HEM806 4.3 43.9 1.0
C3B G:HEM806 4.4 44.4 1.0
CD2 G:LEU583 4.6 37.5 1.0
O G:HOH960 4.7 44.5 1.0

Iron binding site 8 out of 8 in 7oih

Go back to Iron Binding Sites List in 7oih
Iron binding site 8 out of 8 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Fe805

b:58.6
occ:1.00
FE H:HEM805 0.0 58.6 1.0
ND H:HEM805 1.9 58.0 1.0
NA H:HEM805 2.0 57.9 1.0
O H:HOH906 2.0 50.2 1.0
NE2 H:HIS502 2.1 51.0 1.0
NB H:HEM805 2.1 57.1 1.0
NC H:HEM805 2.1 55.5 1.0
C1D H:HEM805 3.0 50.1 1.0
C4D H:HEM805 3.0 54.6 1.0
C1A H:HEM805 3.0 57.6 1.0
C4A H:HEM805 3.1 56.3 1.0
C1B H:HEM805 3.1 56.5 1.0
C4C H:HEM805 3.1 51.1 1.0
CD2 H:HIS502 3.1 44.3 1.0
C4B H:HEM805 3.1 57.9 1.0
CE1 H:HIS502 3.1 52.8 1.0
C1C H:HEM805 3.2 59.3 1.0
CHA H:HEM805 3.4 56.9 1.0
CHD H:HEM805 3.4 51.9 1.0
CHB H:HEM805 3.5 59.3 1.0
CHC H:HEM805 3.5 54.7 1.0
C2D H:HEM805 4.2 49.0 1.0
C3A H:HEM805 4.2 49.2 1.0
C2A H:HEM805 4.2 50.6 1.0
ND1 H:HIS502 4.2 42.4 1.0
CG H:HIS502 4.2 42.4 1.0
C3D H:HEM805 4.2 53.7 1.0
C3C H:HEM805 4.3 52.4 1.0
C2B H:HEM805 4.3 53.7 1.0
C2C H:HEM805 4.3 58.1 1.0
C3B H:HEM805 4.3 60.2 1.0
CD2 H:LEU583 4.6 39.8 1.0
N H:SCN806 5.0 60.7 1.0

Reference:

L.Krawczyk, S.Semwal, J.Soubhye, S.Lemri Ouadriri, M.Prevost, P.Van Antwerpen, G.Roos, J.Bouckaert. Native Glycosylation and Binding of the Antidepressant Paroxetine in A Low-Resolution Crystal Structure of Human Myeloperoxidase. Acta Crystallogr D Struct V. 78 1099 2022BIOL.
ISSN: ISSN 2059-7983
PubMed: 36048150
DOI: 10.1107/S2059798322007082
Page generated: Thu Aug 8 14:23:41 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy