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Iron in PDB 1ix3: Crystal Structure of Rat Heme Oxygenase-1 in Complex with Heme Bound to Cyanide

Enzymatic activity of Crystal Structure of Rat Heme Oxygenase-1 in Complex with Heme Bound to Cyanide

All present enzymatic activity of Crystal Structure of Rat Heme Oxygenase-1 in Complex with Heme Bound to Cyanide:
1.14.99.3;

Protein crystallography data

The structure of Crystal Structure of Rat Heme Oxygenase-1 in Complex with Heme Bound to Cyanide, PDB code: 1ix3 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) 28.80 / 2.00
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 65.700, 65.700, 119.700, 90.00, 90.00, 120.00
R / Rfree (%) 19.9 / 22.6

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Rat Heme Oxygenase-1 in Complex with Heme Bound to Cyanide (pdb code 1ix3). 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 Heme Oxygenase-1 in Complex with Heme Bound to Cyanide, PDB code: 1ix3:

Iron binding site 1 out of 1 in 1ix3

Go back to Iron Binding Sites List in 1ix3
Iron binding site 1 out of 1 in the Crystal Structure of Rat Heme Oxygenase-1 in Complex with Heme Bound to Cyanide


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 Heme Oxygenase-1 in Complex with Heme Bound to Cyanide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe300

b:21.1
occ:1.00
FE A:HEM300 0.0 21.1 1.0
ND A:HEM300 2.0 20.4 1.0
NC A:HEM300 2.0 20.3 1.0
NB A:HEM300 2.0 22.2 1.0
NA A:HEM300 2.0 21.6 1.0
C A:CYN1001 2.1 20.5 1.0
NE2 A:HIS25 2.2 21.6 1.0
C4D A:HEM300 3.0 20.1 1.0
C1D A:HEM300 3.1 18.8 1.0
C4C A:HEM300 3.1 18.9 1.0
C1A A:HEM300 3.1 21.9 1.0
C4B A:HEM300 3.1 21.9 1.0
C1B A:HEM300 3.1 22.2 1.0
C1C A:HEM300 3.1 19.7 1.0
C4A A:HEM300 3.1 22.9 1.0
CE1 A:HIS25 3.1 21.1 1.0
N A:CYN1001 3.1 20.7 1.0
CD2 A:HIS25 3.1 18.9 1.0
CHA A:HEM300 3.4 20.8 1.0
CHD A:HEM300 3.4 18.0 1.0
CHC A:HEM300 3.4 18.6 1.0
CHB A:HEM300 3.4 22.8 1.0
ND1 A:HIS25 4.2 22.2 1.0
CG A:HIS25 4.3 22.2 1.0
C3C A:HEM300 4.3 20.6 1.0
C3D A:HEM300 4.3 18.6 1.0
C2A A:HEM300 4.3 24.7 1.0
C2C A:HEM300 4.3 20.2 1.0
C3A A:HEM300 4.3 22.8 1.0
C2D A:HEM300 4.3 18.4 1.0
C2B A:HEM300 4.3 23.7 1.0
C3B A:HEM300 4.3 23.5 1.0
CA A:GLY143 4.5 18.5 1.0
CA A:GLY139 4.7 19.3 1.0
O A:HOH1089 4.8 19.9 1.0
N A:GLY143 4.9 19.9 1.0

Reference:

M.Sugishima, H.Sakamoto, M.Noguchi, K.Fukuyama. Crystal Structures of Ferrous and Co-, Cn(-)-, and No-Bound Forms of Rat Heme Oxygenase-1 (Ho-1) in Complex with Heme: Structural Implications For Discrimination Between Co and O(2) in Ho-1. Biochemistry V. 42 9898 2003.
ISSN: ISSN 0006-2960
PubMed: 12924938
DOI: 10.1021/BI027268I
Page generated: Sat Aug 3 08:17:47 2024

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