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Iron in PDB 1dvg: Crystal Structure of Rat Heme Oxygenase-1 in Complex with Heme; Seleleno-Methionine Derivative, Mutated at M51T,M93L, M155L,M191L.

Enzymatic activity of Crystal Structure of Rat Heme Oxygenase-1 in Complex with Heme; Seleleno-Methionine Derivative, Mutated at M51T,M93L, M155L,M191L.

All present enzymatic activity of Crystal Structure of Rat Heme Oxygenase-1 in Complex with Heme; Seleleno-Methionine Derivative, Mutated at M51T,M93L, M155L,M191L.:
1.14.99.3;

Protein crystallography data

The structure of Crystal Structure of Rat Heme Oxygenase-1 in Complex with Heme; Seleleno-Methionine Derivative, Mutated at M51T,M93L, M155L,M191L., PDB code: 1dvg was solved by M.Sugishima, Y.Omata, Y.Kakuta, 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) 19.48 / 2.20
Space group P 43
Cell size a, b, c (Å), α, β, γ (°) 54.853, 54.853, 187.558, 90.00, 90.00, 90.00
R / Rfree (%) 21.2 / 25.8

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Rat Heme Oxygenase-1 in Complex with Heme; Seleleno-Methionine Derivative, Mutated at M51T,M93L, M155L,M191L. (pdb code 1dvg). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Rat Heme Oxygenase-1 in Complex with Heme; Seleleno-Methionine Derivative, Mutated at M51T,M93L, M155L,M191L., PDB code: 1dvg:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1dvg

Go back to Iron Binding Sites List in 1dvg
Iron binding site 1 out of 2 in the Crystal Structure of Rat Heme Oxygenase-1 in Complex with Heme; Seleleno-Methionine Derivative, Mutated at M51T,M93L, M155L,M191L.


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; Seleleno-Methionine Derivative, Mutated at M51T,M93L, M155L,M191L. 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
O A:HOH373 1.8 26.9 1.0
ND A:HEM300 2.0 18.9 1.0
NC A:HEM300 2.0 20.0 1.0
NA A:HEM300 2.1 24.0 1.0
NB A:HEM300 2.1 26.1 1.0
NE2 A:HIS25 2.1 15.6 1.0
C4D A:HEM300 3.0 20.2 1.0
C1D A:HEM300 3.0 18.6 1.0
C4C A:HEM300 3.0 20.1 1.0
CE1 A:HIS25 3.0 14.9 1.0
C1C A:HEM300 3.1 22.2 1.0
C1A A:HEM300 3.1 23.8 1.0
C4B A:HEM300 3.1 26.3 1.0
CD2 A:HIS25 3.1 16.2 1.0
C1B A:HEM300 3.1 26.5 1.0
C4A A:HEM300 3.2 25.9 1.0
CHD A:HEM300 3.3 18.4 1.0
CHA A:HEM300 3.4 21.5 1.0
CHC A:HEM300 3.4 23.4 1.0
CHB A:HEM300 3.5 25.7 1.0
ND1 A:HIS25 4.2 16.1 1.0
C3D A:HEM300 4.2 19.3 1.0
C2D A:HEM300 4.2 17.6 1.0
C3C A:HEM300 4.2 20.4 1.0
CG A:HIS25 4.3 15.4 1.0
N A:GLY143 4.3 21.8 1.0
C2C A:HEM300 4.3 21.9 1.0
C2A A:HEM300 4.3 26.8 1.0
C3B A:HEM300 4.4 27.8 1.0
C3A A:HEM300 4.4 26.4 1.0
C2B A:HEM300 4.4 27.3 1.0
CA A:GLY143 4.5 21.5 1.0
CB A:SER142 4.7 21.4 1.0
CA A:GLY139 4.8 20.1 1.0

Iron binding site 2 out of 2 in 1dvg

Go back to Iron Binding Sites List in 1dvg
Iron binding site 2 out of 2 in the Crystal Structure of Rat Heme Oxygenase-1 in Complex with Heme; Seleleno-Methionine Derivative, Mutated at M51T,M93L, M155L,M191L.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Rat Heme Oxygenase-1 in Complex with Heme; Seleleno-Methionine Derivative, Mutated at M51T,M93L, M155L,M191L. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe300

b:29.1
occ:1.00
 FE B:HEM300 0.0 29.1 1.0
NC B:HEM300 1.9 35.8 1.0
NB B:HEM300 2.0 40.7 1.0
O B:HOH370 2.0 36.7 1.0
NE2 B:HIS25 2.1 39.2 1.0
ND B:HEM300 2.1 36.8 1.0
NA B:HEM300 2.1 40.9 1.0
C4C B:HEM300 3.0 35.5 1.0
C1C B:HEM300 3.0 37.5 1.0
CE1 B:HIS25 3.0 39.1 1.0
C4B B:HEM300 3.0 40.0 1.0
C1B B:HEM300 3.1 40.7 1.0
C1D B:HEM300 3.1 35.5 1.0
CD2 B:HIS25 3.1 39.3 1.0
C4D B:HEM300 3.1 37.3 1.0
C1A B:HEM300 3.2 41.2 1.0
C4A B:HEM300 3.2 42.0 1.0
CHC B:HEM300 3.3 38.4 1.0
CHD B:HEM300 3.3 35.1 1.0
CHB B:HEM300 3.5 41.6 1.0
CHA B:HEM300 3.5 38.4 1.0
ND1 B:HIS25 4.1 39.5 1.0
C3C B:HEM300 4.2 35.2 1.0
C2C B:HEM300 4.2 36.4 1.0
CG B:HIS25 4.2 39.6 1.0
C3B B:HEM300 4.3 40.8 1.0
C2B B:HEM300 4.3 41.0 1.0
C2D B:HEM300 4.3 35.9 1.0
N B:GLY143 4.3 34.1 1.0
C3D B:HEM300 4.4 37.0 1.0
C3A B:HEM300 4.4 42.4 1.0
C2A B:HEM300 4.4 42.1 1.0
CB B:SER142 4.6 31.2 1.0
CA B:GLY143 4.7 34.4 1.0
CA B:GLY139 4.7 29.8 1.0
O B:GLY139 5.0 31.2 1.0

Reference:

M.Sugishima, Y.Omata, Y.Kakuta, H.Sakamoto, M.Noguchi, K.Fukuyama. Crystal Structure of Rat Heme Oxygenase-1 in Complex with Heme. Febs Lett. V. 471 61 2000.
ISSN: ISSN 0014-5793
PubMed: 10760513
DOI: 10.1016/S0014-5793(00)01353-3
Page generated: Wed Jul 16 13:27:20 2025

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