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Iron in PDB 1iw0: Crystal Structure of A Heme Oxygenase (Hmuo) From Corynebacterium Diphtheriae Complexed with Heme in the Ferric State

Enzymatic activity of Crystal Structure of A Heme Oxygenase (Hmuo) From Corynebacterium Diphtheriae Complexed with Heme in the Ferric State

All present enzymatic activity of Crystal Structure of A Heme Oxygenase (Hmuo) From Corynebacterium Diphtheriae Complexed with Heme in the Ferric State:
1.14.99.3;

Protein crystallography data

The structure of Crystal Structure of A Heme Oxygenase (Hmuo) From Corynebacterium Diphtheriae Complexed with Heme in the Ferric State, PDB code: 1iw0 was solved by S.Hirotsu, M.Unno, G.C.Chu, D.S.Lee, S.Y.Park, Y.Shiro, M.Ikeda-Saito, Riken Structural Genomics/Proteomics Initiative (Rsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 12.00 / 1.40
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 53.559, 62.838, 107.661, 90.00, 100.86, 90.00
R / Rfree (%) 16.5 / 19.2

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of A Heme Oxygenase (Hmuo) From Corynebacterium Diphtheriae Complexed with Heme in the Ferric State (pdb code 1iw0). 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 A Heme Oxygenase (Hmuo) From Corynebacterium Diphtheriae Complexed with Heme in the Ferric State, PDB code: 1iw0:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in 1iw0

Go back to Iron Binding Sites List in 1iw0
Iron binding site 1 out of 3 in the Crystal Structure of A Heme Oxygenase (Hmuo) From Corynebacterium Diphtheriae Complexed with Heme in the Ferric State


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 A Heme Oxygenase (Hmuo) From Corynebacterium Diphtheriae Complexed with Heme in the Ferric State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe901

b:15.1
occ:1.00
FE A:HEM901 0.0 15.1 1.0
NE2 A:HIS20 2.0 17.4 1.0
NC A:HEM901 2.0 16.6 1.0
NA A:HEM901 2.0 13.9 1.0
ND A:HEM901 2.0 17.5 1.0
NB A:HEM901 2.0 12.7 1.0
O A:HOH1001 2.1 15.9 1.0
C4B A:HEM901 2.9 14.9 1.0
C1C A:HEM901 2.9 17.2 1.0
CE1 A:HIS20 2.9 20.0 1.0
C4D A:HEM901 3.0 18.8 1.0
C4C A:HEM901 3.0 18.5 1.0
CD2 A:HIS20 3.0 17.2 1.0
C1A A:HEM901 3.0 14.8 1.0
C1D A:HEM901 3.1 20.2 1.0
C4A A:HEM901 3.1 12.8 1.0
C1B A:HEM901 3.1 11.9 1.0
CHC A:HEM901 3.3 16.8 1.0
CHD A:HEM901 3.4 19.2 1.0
CHB A:HEM901 3.4 12.0 1.0
CHA A:HEM901 3.5 17.0 1.0
ND1 A:HIS20 4.1 20.4 1.0
CG A:HIS20 4.1 18.1 1.0
C3C A:HEM901 4.2 18.4 1.0
C2C A:HEM901 4.2 18.4 1.0
C3B A:HEM901 4.2 14.3 1.0
O A:HOH1377 4.2 42.1 1.0
C3A A:HEM901 4.2 12.5 1.0
C2D A:HEM901 4.3 23.2 1.0
C2B A:HEM901 4.3 13.0 1.0
O A:HOH1042 4.3 15.6 1.0
C2A A:HEM901 4.3 14.4 1.0
C3D A:HEM901 4.3 23.4 1.0
CA A:GLY135 4.7 13.5 1.0
O A:GLY135 4.7 14.4 1.0

Iron binding site 2 out of 3 in 1iw0

Go back to Iron Binding Sites List in 1iw0
Iron binding site 2 out of 3 in the Crystal Structure of A Heme Oxygenase (Hmuo) From Corynebacterium Diphtheriae Complexed with Heme in the Ferric State


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 A Heme Oxygenase (Hmuo) From Corynebacterium Diphtheriae Complexed with Heme in the Ferric State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe902

b:13.1
occ:1.00
FE B:HEM902 0.0 13.1 1.0
NB B:HEM902 2.0 11.4 1.0
NA B:HEM902 2.0 11.4 1.0
NE2 B:HIS320 2.0 12.4 1.0
ND B:HEM902 2.1 14.2 1.0
NC B:HEM902 2.1 13.9 1.0
O B:HOH1002 2.1 14.4 1.0
C4B B:HEM902 2.9 12.0 1.0
C4D B:HEM902 3.0 14.3 1.0
CD2 B:HIS320 3.0 11.0 1.0
CE1 B:HIS320 3.0 14.2 1.0
C1A B:HEM902 3.0 12.5 1.0
C1C B:HEM902 3.0 14.6 1.0
C4A B:HEM902 3.1 10.2 1.0
C1B B:HEM902 3.1 10.0 1.0
C1D B:HEM902 3.1 15.1 1.0
C4C B:HEM902 3.1 15.6 1.0
CHD B:HEM902 3.4 15.0 1.0
CHB B:HEM902 3.4 10.1 1.0
CHA B:HEM902 3.4 12.9 1.0
CHC B:HEM902 3.4 13.6 1.0
ND1 B:HIS320 4.1 14.9 1.0
CG B:HIS320 4.1 13.0 1.0
C2D B:HEM902 4.2 16.5 1.0
C3B B:HEM902 4.2 12.3 1.0
O B:HOH1443 4.2 15.4 1.0
C3C B:HEM902 4.2 16.3 1.0
C3A B:HEM902 4.2 11.2 1.0
C3D B:HEM902 4.3 17.0 1.0
C2C B:HEM902 4.3 16.6 1.0
C2B B:HEM902 4.3 10.9 1.0
C2A B:HEM902 4.3 11.8 1.0
CA B:GLY435 4.7 12.1 1.0
CA B:GLY439 4.7 22.7 0.5
CA B:GLY439 4.7 22.6 0.5
O B:GLY435 4.7 13.1 1.0
N B:GLY439 4.9 22.1 0.5

Iron binding site 3 out of 3 in 1iw0

Go back to Iron Binding Sites List in 1iw0
Iron binding site 3 out of 3 in the Crystal Structure of A Heme Oxygenase (Hmuo) From Corynebacterium Diphtheriae Complexed with Heme in the Ferric State


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 A Heme Oxygenase (Hmuo) From Corynebacterium Diphtheriae Complexed with Heme in the Ferric State within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe903

b:12.7
occ:1.00
FE C:HEM903 0.0 12.7 1.0
NE2 C:HIS620 2.0 13.8 1.0
NA C:HEM903 2.0 12.1 1.0
NB C:HEM903 2.0 12.0 1.0
ND C:HEM903 2.0 11.9 1.0
NC C:HEM903 2.0 13.6 1.0
O C:HOH1003 2.1 15.7 1.0
CD2 C:HIS620 3.0 14.9 1.0
C1A C:HEM903 3.0 11.8 1.0
CE1 C:HIS620 3.0 15.9 1.0
C1C C:HEM903 3.0 15.0 1.0
C4B C:HEM903 3.0 12.8 1.0
C4D C:HEM903 3.0 12.2 1.0
C1D C:HEM903 3.0 12.1 1.0
C1B C:HEM903 3.1 11.0 1.0
C4A C:HEM903 3.1 10.7 1.0
C4C C:HEM903 3.1 13.9 1.0
CHC C:HEM903 3.4 15.2 1.0
CHA C:HEM903 3.4 12.5 1.0
CHD C:HEM903 3.4 11.8 1.0
CHB C:HEM903 3.4 10.6 1.0
ND1 C:HIS620 4.1 16.6 1.0
CG C:HIS620 4.1 16.3 1.0
O C:HOH1370 4.2 17.9 1.0
C2D C:HEM903 4.2 12.4 1.0
C3B C:HEM903 4.2 13.7 1.0
C2B C:HEM903 4.2 12.6 1.0
C2C C:HEM903 4.2 15.7 1.0
C2A C:HEM903 4.3 11.8 1.0
C3D C:HEM903 4.3 12.8 1.0
C3A C:HEM903 4.3 10.7 1.0
C3C C:HEM903 4.3 15.6 1.0
CA C:GLY735 4.5 11.5 1.0
O C:GLY735 4.7 11.6 1.0

Reference:

S.Hirotsu, G.C.Chu, M.Unno, D.S.Lee, T.Yoshida, S.Y.Park, Y.Shiro, M.Ikeda-Saito. The Crystal Structures of the Ferric and Ferrous Forms of the Heme Complex of Hmuo, A Heme Oxygenase of Corynebacterium Diphtheriae. J.Biol.Chem. V. 279 11937 2004.
ISSN: ISSN 0021-9258
PubMed: 14645223
DOI: 10.1074/JBC.M311631200
Page generated: Sat Aug 3 08:15:37 2024

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