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Iron in PDB 1v8x: Crystal Structure of the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae

Enzymatic activity of Crystal Structure of the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae

All present enzymatic activity of Crystal Structure of the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae:
1.14.99.3;

Protein crystallography data

The structure of Crystal Structure of the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae, PDB code: 1v8x was solved by M.Unno, T.Matsui, G.C.Chu, M.Couture, T.Yoshida, D.L.Rousseau, J.S.Olson, M.Ikeda-Saito, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 1.85
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 54.003, 62.969, 107.490, 90.00, 100.96, 90.00
R / Rfree (%) 15.3 / 19.3

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae (pdb code 1v8x). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Crystal Structure of the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae, PDB code: 1v8x:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in 1v8x

Go back to Iron Binding Sites List in 1v8x
Iron binding site 1 out of 3 in the Crystal Structure of the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe901

b:16.9
occ:1.00
FE A:HEM901 0.0 16.9 1.0
O1 A:OXY5001 1.9 31.9 1.0
ND A:HEM901 2.0 17.0 1.0
NA A:HEM901 2.0 15.6 1.0
NC A:HEM901 2.1 16.6 1.0
NB A:HEM901 2.1 14.0 1.0
NE2 A:HIS20 2.2 19.4 1.0
O2 A:OXY5001 2.6 31.4 1.0
C4A A:HEM901 3.0 12.3 1.0
C4D A:HEM901 3.0 16.5 1.0
C4B A:HEM901 3.0 13.7 1.0
C1D A:HEM901 3.1 20.9 1.0
C1C A:HEM901 3.1 15.8 1.0
C1B A:HEM901 3.1 13.7 1.0
C1A A:HEM901 3.1 15.1 1.0
C4C A:HEM901 3.1 18.3 1.0
CD2 A:HIS20 3.2 19.9 1.0
CE1 A:HIS20 3.2 25.4 1.0
CHC A:HEM901 3.4 14.9 1.0
CHB A:HEM901 3.4 14.4 1.0
CHA A:HEM901 3.4 14.4 1.0
CHD A:HEM901 3.5 19.5 1.0
N A:GLY139 4.2 18.0 1.0
C3A A:HEM901 4.3 12.5 1.0
C3B A:HEM901 4.3 12.1 1.0
C2D A:HEM901 4.3 22.1 1.0
C2B A:HEM901 4.3 10.7 1.0
C3C A:HEM901 4.3 19.9 1.0
C3D A:HEM901 4.3 17.8 1.0
C2C A:HEM901 4.3 17.3 1.0
CA A:GLY139 4.3 18.8 1.0
ND1 A:HIS20 4.3 24.6 1.0
C2A A:HEM901 4.3 14.6 1.0
CG A:HIS20 4.3 22.8 1.0
CA A:GLY135 4.6 15.2 1.0
O A:GLY135 4.9 13.3 1.0
O A:HOH5064 4.9 15.8 1.0
CB A:SER138 5.0 17.9 1.0

Iron binding site 2 out of 3 in 1v8x

Go back to Iron Binding Sites List in 1v8x
Iron binding site 2 out of 3 in the Crystal Structure of the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe902

b:21.9
occ:1.00
FE B:HEM902 0.0 21.9 1.0
O1 B:OXY5002 2.0 26.2 1.0
ND B:HEM902 2.0 24.5 1.0
NB B:HEM902 2.0 18.8 1.0
NA B:HEM902 2.0 17.8 1.0
NC B:HEM902 2.1 24.5 1.0
NE2 B:HIS320 2.1 23.4 1.0
O2 B:OXY5002 2.6 32.5 1.0
C4B B:HEM902 3.0 21.9 1.0
C4D B:HEM902 3.0 21.8 1.0
C1D B:HEM902 3.0 23.8 1.0
C1A B:HEM902 3.0 18.1 1.0
CD2 B:HIS320 3.1 20.8 1.0
C1B B:HEM902 3.1 16.8 1.0
C1C B:HEM902 3.1 25.9 1.0
C4A B:HEM902 3.1 17.1 1.0
CE1 B:HIS320 3.2 23.9 1.0
C4C B:HEM902 3.2 29.4 1.0
CHA B:HEM902 3.4 20.9 1.0
CHC B:HEM902 3.4 22.2 1.0
CHB B:HEM902 3.5 16.3 1.0
CHD B:HEM902 3.5 30.2 1.0
C3B B:HEM902 4.2 20.4 1.0
C2B B:HEM902 4.2 15.6 1.0
C3D B:HEM902 4.2 29.1 1.0
CG B:HIS320 4.2 23.7 1.0
C2D B:HEM902 4.2 28.6 1.0
ND1 B:HIS320 4.2 26.0 1.0
C3A B:HEM902 4.3 16.1 1.0
C2A B:HEM902 4.3 19.2 1.0
CA B:GLY439 4.3 23.9 1.0
C2C B:HEM902 4.3 31.1 1.0
N B:GLY439 4.4 22.9 1.0
C3C B:HEM902 4.4 30.9 1.0
CA B:GLY435 4.6 15.1 1.0
O B:HOH5083 4.6 20.5 1.0
O B:GLY435 4.8 15.6 1.0

Iron binding site 3 out of 3 in 1v8x

Go back to Iron Binding Sites List in 1v8x
Iron binding site 3 out of 3 in the Crystal Structure of the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe903

b:20.6
occ:1.00
FE C:HEM903 0.0 20.6 1.0
O1 C:OXY5003 2.0 33.2 1.0
NA C:HEM903 2.0 20.1 1.0
ND C:HEM903 2.0 19.0 1.0
NE2 C:HIS620 2.0 24.2 1.0
NB C:HEM903 2.0 20.3 1.0
NC C:HEM903 2.1 20.4 1.0
O2 C:OXY5003 2.5 33.7 1.0
CD2 C:HIS620 2.9 26.5 1.0
C1D C:HEM903 3.0 21.7 1.0
C4A C:HEM903 3.0 18.7 1.0
C1B C:HEM903 3.0 19.6 1.0
C4B C:HEM903 3.1 19.8 1.0
C4D C:HEM903 3.1 20.2 1.0
C4C C:HEM903 3.1 22.0 1.0
C1A C:HEM903 3.1 18.0 1.0
CE1 C:HIS620 3.1 27.0 1.0
C1C C:HEM903 3.2 19.4 1.0
CHB C:HEM903 3.4 19.4 1.0
CHD C:HEM903 3.4 24.4 1.0
CHC C:HEM903 3.5 20.9 1.0
CHA C:HEM903 3.5 18.1 1.0
CG C:HIS620 4.1 29.2 1.0
ND1 C:HIS620 4.2 28.9 1.0
C3A C:HEM903 4.2 19.2 1.0
C2D C:HEM903 4.2 23.3 1.0
C2B C:HEM903 4.2 17.6 1.0
C3B C:HEM903 4.3 22.0 1.0
C2A C:HEM903 4.3 19.1 1.0
C3D C:HEM903 4.3 22.2 1.0
C3C C:HEM903 4.4 25.6 1.0
CA C:GLY735 4.4 19.3 1.0
C2C C:HEM903 4.4 25.2 1.0
O C:HOH218 4.5 22.3 1.0
O C:GLY735 4.7 19.9 1.0
C C:GLY735 5.0 19.1 1.0

Reference:

M.Unno, T.Matsui, G.C.Chu, M.Couture, T.Yoshida, D.L.Rousseau, J.S.Olson, M.Ikeda-Saito. Crystal Structure of the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae: Implications For Heme Oxygenase Function. J.Biol.Chem. V. 279 21055 2004.
ISSN: ISSN 0021-9258
PubMed: 14966119
DOI: 10.1074/JBC.M400491200
Page generated: Sat Aug 3 16:10:45 2024

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