Atomistry » Iron » PDB 4g39-4gl5 » 4g8u
Atomistry »
  Iron »
    PDB 4g39-4gl5 »
      4g8u »

Iron in PDB 4g8u: Rat Heme Oxygenase-1 in Complex with Heme and O2 with 13 Hr Illumination: Laser Off

Enzymatic activity of Rat Heme Oxygenase-1 in Complex with Heme and O2 with 13 Hr Illumination: Laser Off

All present enzymatic activity of Rat Heme Oxygenase-1 in Complex with Heme and O2 with 13 Hr Illumination: Laser Off:
1.14.99.3;

Protein crystallography data

The structure of Rat Heme Oxygenase-1 in Complex with Heme and O2 with 13 Hr Illumination: Laser Off, PDB code: 4g8u 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) 28.67 / 2.10
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 65.172, 65.172, 120.643, 90.00, 90.00, 120.00
R / Rfree (%) 15.5 / 18.8

Iron Binding Sites:

The binding sites of Iron atom in the Rat Heme Oxygenase-1 in Complex with Heme and O2 with 13 Hr Illumination: Laser Off (pdb code 4g8u). 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 O2 with 13 Hr Illumination: Laser Off, PDB code: 4g8u:

Iron binding site 1 out of 1 in 4g8u

Go back to Iron Binding Sites List in 4g8u
Iron binding site 1 out of 1 in the Rat Heme Oxygenase-1 in Complex with Heme and O2 with 13 Hr Illumination: 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 O2 with 13 Hr Illumination: Laser Off within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe301

b:34.2
occ:1.00
FE A:HEM301 0.0 34.2 1.0
O1 A:OXY302 1.9 32.9 0.8
NC A:HEM301 1.9 31.2 1.0
NA A:HEM301 2.0 35.2 1.0
NE2 A:HIS25 2.0 32.9 1.0
ND A:HEM301 2.1 31.6 1.0
NB A:HEM301 2.1 35.9 1.0
O2 A:OXY302 2.6 44.8 0.8
C4C A:HEM301 2.9 28.6 1.0
C1C A:HEM301 3.0 31.5 1.0
CD2 A:HIS25 3.0 29.9 1.0
CE1 A:HIS25 3.0 32.6 1.0
C4D A:HEM301 3.0 31.3 1.0
C1D A:HEM301 3.0 30.1 1.0
C4B A:HEM301 3.0 33.8 1.0
C4A A:HEM301 3.1 35.5 1.0
C1A A:HEM301 3.1 35.2 1.0
C1B A:HEM301 3.1 37.2 1.0
CHD A:HEM301 3.4 28.4 1.0
CHC A:HEM301 3.4 31.9 1.0
CHA A:HEM301 3.4 34.6 1.0
CHB A:HEM301 3.5 35.2 1.0
ND1 A:HIS25 4.2 35.4 1.0
C3C A:HEM301 4.2 30.7 1.0
CG A:HIS25 4.2 31.6 1.0
N A:GLY143 4.3 34.0 1.0
C2C A:HEM301 4.3 31.3 1.0
C3D A:HEM301 4.3 30.9 1.0
C3B A:HEM301 4.3 37.5 1.0
CA A:GLY139 4.4 32.8 1.0
C2D A:HEM301 4.4 30.8 1.0
C3A A:HEM301 4.4 35.9 1.0
C2A A:HEM301 4.4 35.7 1.0
C2B A:HEM301 4.4 37.8 1.0
O A:HOH484 4.5 48.2 1.0
CA A:GLY143 4.6 36.9 1.0
O A:HOH486 4.7 50.7 1.0
CB A:SER142 4.7 35.3 1.0
O A:GLY139 4.9 30.5 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: Sun Dec 13 15:35:09 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy