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Iron in PDB 1vgi: Crystal Structure of Xenon Bound Rat Heme-Heme Oxygenase-1 Complex

Enzymatic activity of Crystal Structure of Xenon Bound Rat Heme-Heme Oxygenase-1 Complex

All present enzymatic activity of Crystal Structure of Xenon Bound Rat Heme-Heme Oxygenase-1 Complex:
1.14.99.3;

Protein crystallography data

The structure of Crystal Structure of Xenon Bound Rat Heme-Heme Oxygenase-1 Complex, PDB code: 1vgi was solved by M.Sugishima, H.Sakamoto, M.Noguchi, K.Fukuyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.90
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 65.100, 65.100, 120.500, 90.00, 90.00, 120.00
R / Rfree (%) 20.1 / 21.7

Other elements in 1vgi:

The structure of Crystal Structure of Xenon Bound Rat Heme-Heme Oxygenase-1 Complex also contains other interesting chemical elements:

Xenon (Xe) 3 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Xenon Bound Rat Heme-Heme Oxygenase-1 Complex (pdb code 1vgi). 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 Xenon Bound Rat Heme-Heme Oxygenase-1 Complex, PDB code: 1vgi:

Iron binding site 1 out of 1 in 1vgi

Go back to Iron Binding Sites List in 1vgi
Iron binding site 1 out of 1 in the Crystal Structure of Xenon Bound Rat Heme-Heme Oxygenase-1 Complex


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 Xenon Bound Rat Heme-Heme Oxygenase-1 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe300

b:28.1
occ:1.00
 FE A:HEM300 0.0 28.1 1.0
NB A:HEM300 2.0 32.0 1.0
NC A:HEM300 2.0 27.8 1.0
ND A:HEM300 2.0 28.4 1.0
NA A:HEM300 2.0 31.8 1.0
O A:HOH369 2.1 33.2 1.0
NE2 A:HIS25 2.1 29.0 1.0
C4D A:HEM300 3.0 29.2 1.0
C1B A:HEM300 3.0 33.5 1.0
C1D A:HEM300 3.0 26.6 1.0
C4C A:HEM300 3.0 26.3 1.0
C4B A:HEM300 3.0 32.0 1.0
C4A A:HEM300 3.0 32.8 1.0
C1C A:HEM300 3.1 29.1 1.0
C1A A:HEM300 3.1 32.0 1.0
CD2 A:HIS25 3.1 28.6 1.0
CE1 A:HIS25 3.1 30.7 1.0
CHD A:HEM300 3.4 25.9 1.0
CHB A:HEM300 3.4 34.1 1.0
CHA A:HEM300 3.4 30.1 1.0
CHC A:HEM300 3.4 28.6 1.0
ND1 A:HIS25 4.2 31.7 1.0
CG A:HIS25 4.2 30.2 1.0
N A:GLY143 4.3 37.5 1.0
C3C A:HEM300 4.3 29.7 1.0
C2B A:HEM300 4.3 35.9 1.0
C3D A:HEM300 4.3 29.3 1.0
C3B A:HEM300 4.3 35.2 1.0
C2D A:HEM300 4.3 27.2 1.0
C3A A:HEM300 4.3 35.8 1.0
C2C A:HEM300 4.3 29.3 1.0
C2A A:HEM300 4.3 36.2 1.0
CA A:GLY143 4.5 37.9 1.0
CA A:GLY139 4.6 30.9 1.0
CB A:SER142 4.7 37.6 1.0
O A:GLY139 4.9 31.4 1.0
O A:HOH367 5.0 59.4 1.0

Reference:

M.Sugishima, H.Sakamoto, M.Noguchi, K.Fukuyama. Co-Trapping Site in Heme Oxygenase Revealed By Photolysis of Its Co-Bound Heme Complex: Mechanism of Escaping From Product Inhibition J.Mol.Biol. V. 341 7 2004.
ISSN: ISSN 0022-2836
PubMed: 15312758
DOI: 10.1016/J.JMB.2004.05.048
Page generated: Sun Dec 13 14:34:20 2020

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