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Iron in PDB 1ivj: Crystal Structure of Rat Hemeoxygenase-1 in Complex with Heme and Azide.

Enzymatic activity of Crystal Structure of Rat Hemeoxygenase-1 in Complex with Heme and Azide.

All present enzymatic activity of Crystal Structure of Rat Hemeoxygenase-1 in Complex with Heme and Azide.:
1.14.99.3;

Protein crystallography data

The structure of Crystal Structure of Rat Hemeoxygenase-1 in Complex with Heme and Azide., PDB code: 1ivj was solved by M.Sugishima, H.Sakamoto, Y.Omata, S.Hayashi, M.Noguchi, K.Fukuyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.90
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 65.010, 65.010, 120.250, 90.00, 90.00, 120.00
R / Rfree (%) 18.9 / 21.9

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Rat Hemeoxygenase-1 in Complex with Heme and Azide. (pdb code 1ivj). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of Rat Hemeoxygenase-1 in Complex with Heme and Azide., PDB code: 1ivj:

Iron binding site 1 out of 1 in 1ivj

Go back to Iron Binding Sites List in 1ivj
Iron binding site 1 out of 1 in the Crystal Structure of Rat Hemeoxygenase-1 in Complex with Heme and Azide.


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 Rat Hemeoxygenase-1 in Complex with Heme and Azide. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe300

b:17.1
occ:1.00
FE A:HEM300 0.0 17.1 1.0
ND A:HEM300 2.0 18.0 1.0
NB A:HEM300 2.0 17.2 1.0
NC A:HEM300 2.0 17.8 1.0
NA A:HEM300 2.0 17.4 1.0
NE2 A:HIS25 2.1 16.6 1.0
N3 A:AZI1001 2.2 21.1 1.0
N2 A:AZI1001 2.8 27.5 1.0
C4D A:HEM300 3.0 18.2 1.0
C1D A:HEM300 3.0 17.3 1.0
C1B A:HEM300 3.0 18.2 1.0
C4B A:HEM300 3.0 18.3 1.0
C4C A:HEM300 3.0 16.0 1.0
C1A A:HEM300 3.1 17.2 1.0
C4A A:HEM300 3.1 18.1 1.0
C1C A:HEM300 3.1 17.3 1.0
CE1 A:HIS25 3.1 17.8 1.0
CD2 A:HIS25 3.1 17.2 1.0
CHA A:HEM300 3.4 17.1 1.0
CHD A:HEM300 3.4 16.5 1.0
CHC A:HEM300 3.4 18.0 1.0
CHB A:HEM300 3.4 16.7 1.0
N1 A:AZI1001 3.8 26.7 1.0
ND1 A:HIS25 4.2 17.4 1.0
CG A:HIS25 4.3 16.5 1.0
C3D A:HEM300 4.3 18.1 1.0
C2B A:HEM300 4.3 19.0 1.0
C3C A:HEM300 4.3 16.7 1.0
C2D A:HEM300 4.3 16.8 1.0
C3B A:HEM300 4.3 20.0 1.0
C2A A:HEM300 4.3 19.3 1.0
C2C A:HEM300 4.3 17.9 1.0
C3A A:HEM300 4.3 19.6 1.0
N A:GLY143 4.3 16.0 1.0
CA A:GLY139 4.6 15.9 1.0
CB A:SER142 4.6 15.9 1.0
CA A:GLY143 4.6 15.9 1.0
O A:HOH1160 4.8 39.8 1.0
O A:GLY139 5.0 16.5 1.0

Reference:

M.Sugishima, H.Sakamoto, Y.Omata, S.Hayashi, M.Noguchi, K.Fukuyama. Crystal Structure of Rat Heme Oxygenase-1 in Complex with Heme Bound to Azide. Implication For Regiospecific Hydroxylation of Heme at the Alpha -Meso Carbon J.Biol.Chem. V. 277 45086 2002.
ISSN: ISSN 0021-9258
PubMed: 12235152
DOI: 10.1074/JBC.M207267200
Page generated: Wed Jul 16 16:22:17 2025

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