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Iron in PDB 4g7p: Rat Heme Oxygenase-1 in Complex with Heme and Co with 1 Hr Illumination at 100 K: Laser Off

Enzymatic activity of Rat Heme Oxygenase-1 in Complex with Heme and Co with 1 Hr Illumination at 100 K: Laser Off

All present enzymatic activity of Rat Heme Oxygenase-1 in Complex with Heme and Co with 1 Hr Illumination at 100 K: Laser Off:
1.14.99.3;

Protein crystallography data

The structure of Rat Heme Oxygenase-1 in Complex with Heme and Co with 1 Hr Illumination at 100 K: Laser Off, PDB code: 4g7p was solved by M.Sugishima, K.Moffat, M.Noguchi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.80 / 1.90
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 65.841, 65.841, 120.268, 90.00, 90.00, 120.00
R / Rfree (%) 16.6 / 20.1

Iron Binding Sites:

The binding sites of Iron atom in the Rat Heme Oxygenase-1 in Complex with Heme and Co with 1 Hr Illumination at 100 K: Laser Off (pdb code 4g7p). 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 Rat Heme Oxygenase-1 in Complex with Heme and Co with 1 Hr Illumination at 100 K: Laser Off, PDB code: 4g7p:

Iron binding site 1 out of 1 in 4g7p

Go back to Iron Binding Sites List in 4g7p
Iron binding site 1 out of 1 in the Rat Heme Oxygenase-1 in Complex with Heme and Co with 1 Hr Illumination at 100 K: Laser Off


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Rat Heme Oxygenase-1 in Complex with Heme and Co with 1 Hr Illumination at 100 K: Laser Off within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe300

b:28.6
occ:1.00
 FE A:HEM300 0.0 28.6 1.0
NA A:HEM300 2.0 27.6 1.0
NC A:HEM300 2.0 25.7 1.0
C A:CMO301 2.0 26.5 1.0
ND A:HEM300 2.1 27.2 1.0
NB A:HEM300 2.1 29.0 1.0
NE2 A:HIS25 2.3 27.4 1.0
C4A A:HEM300 3.0 29.2 1.0
C4C A:HEM300 3.0 24.3 1.0
C1C A:HEM300 3.0 27.5 1.0
C4B A:HEM300 3.1 29.3 1.0
C1D A:HEM300 3.1 24.2 1.0
O A:CMO301 3.1 34.0 1.0
C1A A:HEM300 3.1 29.3 1.0
CD2 A:HIS25 3.2 26.2 1.0
C4D A:HEM300 3.2 26.7 1.0
C1B A:HEM300 3.2 28.1 1.0
CE1 A:HIS25 3.3 29.1 1.0
CHD A:HEM300 3.4 23.9 1.0
CHC A:HEM300 3.4 26.6 1.0
CHB A:HEM300 3.5 29.6 1.0
CHA A:HEM300 3.7 26.2 1.0
C3C A:HEM300 4.2 26.4 1.0
C3A A:HEM300 4.3 32.9 1.0
C2C A:HEM300 4.3 25.0 1.0
C2A A:HEM300 4.3 29.9 1.0
CG A:HIS25 4.4 27.4 1.0
C3B A:HEM300 4.4 31.0 1.0
ND1 A:HIS25 4.4 29.0 1.0
C2D A:HEM300 4.4 25.3 1.0
C3D A:HEM300 4.4 26.5 1.0
CA A:GLY143 4.4 25.3 1.0
C2B A:HEM300 4.5 28.6 1.0
CA A:GLY139 4.5 19.7 1.0
N A:GLY143 4.6 25.4 1.0
O A:HOH432 4.7 31.8 1.0
O A:HOH454 4.9 41.0 1.0
O A:GLY139 4.9 21.4 1.0

Reference:

M.Sugishima, K.Moffat, M.Noguchi. Discrimination Between Co and O2 in Heme Oxygenase: Comparison of Static Structures and Dynamic Conformation Changes Following Co Photolysis Biochemistry 2012.
ISSN: ISSN 0006-2960
PubMed: 23043644
DOI: 10.1021/BI301175X
Page generated: Tue Aug 5 10:35:14 2025

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