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:
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: Sat Aug 3 16:31:02 2024
|