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Iron in PDB 1we1: Crystal Structure of Heme Oxygenase-1 From Cyanobacterium Synechocystis Sp. PCC6803 in Complex with Heme

Enzymatic activity of Crystal Structure of Heme Oxygenase-1 From Cyanobacterium Synechocystis Sp. PCC6803 in Complex with Heme

All present enzymatic activity of Crystal Structure of Heme Oxygenase-1 From Cyanobacterium Synechocystis Sp. PCC6803 in Complex with Heme:
1.14.99.3;

Protein crystallography data

The structure of Crystal Structure of Heme Oxygenase-1 From Cyanobacterium Synechocystis Sp. PCC6803 in Complex with Heme, PDB code: 1we1 was solved by M.Sugishima, C.T.Migita, X.Zhang, T.Yoshida, K.Fukuyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 110.790, 113.730, 109.700, 90.00, 112.26, 90.00
R / Rfree (%) 22 / 26.9

Other elements in 1we1:

The structure of Crystal Structure of Heme Oxygenase-1 From Cyanobacterium Synechocystis Sp. PCC6803 in Complex with Heme also contains other interesting chemical elements:

Chlorine (Cl) 5 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Heme Oxygenase-1 From Cyanobacterium Synechocystis Sp. PCC6803 in Complex with Heme (pdb code 1we1). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of Heme Oxygenase-1 From Cyanobacterium Synechocystis Sp. PCC6803 in Complex with Heme, PDB code: 1we1:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1we1

Go back to Iron Binding Sites List in 1we1
Iron binding site 1 out of 4 in the Crystal Structure of Heme Oxygenase-1 From Cyanobacterium Synechocystis Sp. PCC6803 in Complex with Heme


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 Heme Oxygenase-1 From Cyanobacterium Synechocystis Sp. PCC6803 in Complex with Heme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe300

b:47.2
occ:1.00
FE A:HEM300 0.0 47.2 1.0
O A:HOH1006 1.8 47.3 1.0
ND A:HEM300 2.0 50.1 1.0
NB A:HEM300 2.0 46.8 1.0
NA A:HEM300 2.0 49.1 1.0
NC A:HEM300 2.0 50.4 1.0
NE2 A:HIS17 2.0 42.7 1.0
CD2 A:HIS17 2.9 41.8 1.0
C4D A:HEM300 3.0 50.7 1.0
C1D A:HEM300 3.0 53.1 1.0
C1A A:HEM300 3.0 48.6 1.0
C1B A:HEM300 3.0 46.8 1.0
C4A A:HEM300 3.0 48.0 1.0
C4B A:HEM300 3.0 46.9 1.0
C4C A:HEM300 3.1 50.9 1.0
C1C A:HEM300 3.1 49.1 1.0
CE1 A:HIS17 3.1 41.2 1.0
CHA A:HEM300 3.4 50.5 1.0
CHB A:HEM300 3.4 46.8 1.0
CHD A:HEM300 3.4 51.1 1.0
CHC A:HEM300 3.4 48.7 1.0
CG A:HIS17 4.1 43.1 1.0
ND1 A:HIS17 4.1 39.6 1.0
C3D A:HEM300 4.3 53.7 1.0
C2D A:HEM300 4.3 52.5 1.0
C2A A:HEM300 4.3 48.5 1.0
C2B A:HEM300 4.3 46.2 1.0
C3C A:HEM300 4.3 52.7 1.0
C3B A:HEM300 4.3 47.4 1.0
C3A A:HEM300 4.3 48.0 1.0
C2C A:HEM300 4.3 51.9 1.0
CA A:GLY130 4.7 49.4 1.0
O A:GLY130 4.7 50.3 1.0

Iron binding site 2 out of 4 in 1we1

Go back to Iron Binding Sites List in 1we1
Iron binding site 2 out of 4 in the Crystal Structure of Heme Oxygenase-1 From Cyanobacterium Synechocystis Sp. PCC6803 in Complex with Heme


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 Heme Oxygenase-1 From Cyanobacterium Synechocystis Sp. PCC6803 in Complex with Heme within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe300

b:38.6
occ:1.00
FE B:HEM300 0.0 38.6 1.0
ND B:HEM300 2.0 41.0 1.0
NB B:HEM300 2.0 39.4 1.0
NC B:HEM300 2.0 40.9 1.0
NE2 B:HIS17 2.0 35.6 1.0
NA B:HEM300 2.0 38.7 1.0
O B:HOH1007 2.1 30.0 1.0
CD2 B:HIS17 2.9 34.1 1.0
C4D B:HEM300 3.0 40.5 1.0
CE1 B:HIS17 3.0 31.3 1.0
C1A B:HEM300 3.0 40.6 1.0
C4B B:HEM300 3.0 38.5 1.0
C1B B:HEM300 3.0 39.7 1.0
C1D B:HEM300 3.0 43.6 1.0
C4A B:HEM300 3.0 39.4 1.0
C4C B:HEM300 3.1 43.0 1.0
C1C B:HEM300 3.1 39.4 1.0
CHA B:HEM300 3.4 40.0 1.0
CHC B:HEM300 3.4 37.9 1.0
CHD B:HEM300 3.4 42.8 1.0
CHB B:HEM300 3.4 40.9 1.0
CG B:HIS17 4.1 32.8 1.0
ND1 B:HIS17 4.1 34.0 1.0
C3C B:HEM300 4.3 43.3 1.0
C3D B:HEM300 4.3 44.1 1.0
C2B B:HEM300 4.3 38.0 1.0
C2A B:HEM300 4.3 41.3 1.0
C3B B:HEM300 4.3 39.5 1.0
C3A B:HEM300 4.3 38.8 1.0
C2D B:HEM300 4.3 44.0 1.0
C2C B:HEM300 4.3 43.7 1.0
O B:HOH1029 4.6 38.7 1.0
O B:GLY130 4.7 40.4 1.0
CA B:GLY130 4.7 36.4 1.0

Iron binding site 3 out of 4 in 1we1

Go back to Iron Binding Sites List in 1we1
Iron binding site 3 out of 4 in the Crystal Structure of Heme Oxygenase-1 From Cyanobacterium Synechocystis Sp. PCC6803 in Complex with Heme


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of Heme Oxygenase-1 From Cyanobacterium Synechocystis Sp. PCC6803 in Complex with Heme within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe300

b:37.8
occ:1.00
FE C:HEM300 0.0 37.8 1.0
NE2 C:HIS17 1.9 35.1 1.0
O C:HOH1008 1.9 36.0 1.0
ND C:HEM300 2.0 39.3 1.0
NB C:HEM300 2.0 39.7 1.0
NC C:HEM300 2.0 42.5 1.0
NA C:HEM300 2.0 39.3 1.0
CE1 C:HIS17 2.8 35.4 1.0
CD2 C:HIS17 3.0 36.2 1.0
C4D C:HEM300 3.0 40.1 1.0
C1D C:HEM300 3.0 43.2 1.0
C1B C:HEM300 3.0 41.3 1.0
C4B C:HEM300 3.0 42.1 1.0
C4C C:HEM300 3.0 43.0 1.0
C4A C:HEM300 3.1 38.8 1.0
C1A C:HEM300 3.1 38.0 1.0
C1C C:HEM300 3.1 41.9 1.0
CHD C:HEM300 3.4 42.0 1.0
CHA C:HEM300 3.4 38.9 1.0
CHC C:HEM300 3.4 42.1 1.0
CHB C:HEM300 3.4 39.9 1.0
ND1 C:HIS17 3.9 38.0 1.0
CG C:HIS17 4.0 36.8 1.0
O C:HOH1031 4.2 47.1 1.0
C3D C:HEM300 4.3 42.4 1.0
C2D C:HEM300 4.3 44.9 1.0
C3C C:HEM300 4.3 45.0 1.0
C2B C:HEM300 4.3 41.7 1.0
C3B C:HEM300 4.3 40.1 1.0
C2A C:HEM300 4.3 40.1 1.0
C3A C:HEM300 4.3 40.2 1.0
C2C C:HEM300 4.3 45.9 1.0
O C:GLY130 4.6 41.8 1.0
CA C:GLY130 4.8 41.7 1.0

Iron binding site 4 out of 4 in 1we1

Go back to Iron Binding Sites List in 1we1
Iron binding site 4 out of 4 in the Crystal Structure of Heme Oxygenase-1 From Cyanobacterium Synechocystis Sp. PCC6803 in Complex with Heme


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of Heme Oxygenase-1 From Cyanobacterium Synechocystis Sp. PCC6803 in Complex with Heme within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe300

b:44.8
occ:1.00
FE D:HEM300 0.0 44.8 1.0
O D:HOH1009 2.0 40.6 1.0
ND D:HEM300 2.0 46.6 1.0
NB D:HEM300 2.0 44.9 1.0
NC D:HEM300 2.0 45.8 1.0
NA D:HEM300 2.0 45.2 1.0
NE2 D:HIS17 2.1 45.7 1.0
C4D D:HEM300 3.0 47.9 1.0
CD2 D:HIS17 3.0 47.1 1.0
C1D D:HEM300 3.0 48.7 1.0
C1B D:HEM300 3.0 44.3 1.0
C4B D:HEM300 3.0 45.3 1.0
C4C D:HEM300 3.0 47.3 1.0
C1A D:HEM300 3.1 45.5 1.0
C4A D:HEM300 3.1 44.6 1.0
C1C D:HEM300 3.1 46.6 1.0
CE1 D:HIS17 3.1 46.2 1.0
CHA D:HEM300 3.4 47.1 1.0
CHD D:HEM300 3.4 46.6 1.0
CHC D:HEM300 3.4 45.6 1.0
CHB D:HEM300 3.4 43.8 1.0
CG D:HIS17 4.2 47.6 1.0
ND1 D:HIS17 4.2 47.9 1.0
C3C D:HEM300 4.3 49.5 1.0
C3D D:HEM300 4.3 51.5 1.0
C3B D:HEM300 4.3 44.8 1.0
C2B D:HEM300 4.3 44.5 1.0
C2A D:HEM300 4.3 46.6 1.0
C2D D:HEM300 4.3 50.1 1.0
C2C D:HEM300 4.3 50.4 1.0
C3A D:HEM300 4.3 46.3 1.0
CA D:GLY130 4.8 46.8 1.0
O D:GLY130 4.9 48.2 1.0

Reference:

M.Sugishima, C.T.Migita, X.Zhang, T.Yoshida, K.Fukuyama. Crystal Structure of Heme Oxygenase-1 From Cyanobacterium Synechocystis Sp. Pcc 6803 in Complex with Heme Eur.J.Biochem. V. 271 4517 2004.
ISSN: ISSN 0014-2956
PubMed: 15560792
DOI: 10.1111/J.1432-1033.2004.04411.X
Page generated: Sun Dec 13 14:35:08 2020

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