Iron in PDB 1v8x: Crystal Structure of the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae
Enzymatic activity of Crystal Structure of the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae
All present enzymatic activity of Crystal Structure of the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae:
1.14.99.3;
Protein crystallography data
The structure of Crystal Structure of the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae, PDB code: 1v8x
was solved by
M.Unno,
T.Matsui,
G.C.Chu,
M.Couture,
T.Yoshida,
D.L.Rousseau,
J.S.Olson,
M.Ikeda-Saito,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
40.00 /
1.85
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
54.003,
62.969,
107.490,
90.00,
100.96,
90.00
|
R / Rfree (%)
|
15.3 /
19.3
|
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae
(pdb code 1v8x). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the
Crystal Structure of the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae, PDB code: 1v8x:
Jump to Iron binding site number:
1;
2;
3;
Iron binding site 1 out
of 3 in 1v8x
Go back to
Iron Binding Sites List in 1v8x
Iron binding site 1 out
of 3 in the Crystal Structure of the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae
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 the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe901
b:16.9
occ:1.00
|
FE
|
A:HEM901
|
0.0
|
16.9
|
1.0
|
O1
|
A:OXY5001
|
1.9
|
31.9
|
1.0
|
ND
|
A:HEM901
|
2.0
|
17.0
|
1.0
|
NA
|
A:HEM901
|
2.0
|
15.6
|
1.0
|
NC
|
A:HEM901
|
2.1
|
16.6
|
1.0
|
NB
|
A:HEM901
|
2.1
|
14.0
|
1.0
|
NE2
|
A:HIS20
|
2.2
|
19.4
|
1.0
|
O2
|
A:OXY5001
|
2.6
|
31.4
|
1.0
|
C4A
|
A:HEM901
|
3.0
|
12.3
|
1.0
|
C4D
|
A:HEM901
|
3.0
|
16.5
|
1.0
|
C4B
|
A:HEM901
|
3.0
|
13.7
|
1.0
|
C1D
|
A:HEM901
|
3.1
|
20.9
|
1.0
|
C1C
|
A:HEM901
|
3.1
|
15.8
|
1.0
|
C1B
|
A:HEM901
|
3.1
|
13.7
|
1.0
|
C1A
|
A:HEM901
|
3.1
|
15.1
|
1.0
|
C4C
|
A:HEM901
|
3.1
|
18.3
|
1.0
|
CD2
|
A:HIS20
|
3.2
|
19.9
|
1.0
|
CE1
|
A:HIS20
|
3.2
|
25.4
|
1.0
|
CHC
|
A:HEM901
|
3.4
|
14.9
|
1.0
|
CHB
|
A:HEM901
|
3.4
|
14.4
|
1.0
|
CHA
|
A:HEM901
|
3.4
|
14.4
|
1.0
|
CHD
|
A:HEM901
|
3.5
|
19.5
|
1.0
|
N
|
A:GLY139
|
4.2
|
18.0
|
1.0
|
C3A
|
A:HEM901
|
4.3
|
12.5
|
1.0
|
C3B
|
A:HEM901
|
4.3
|
12.1
|
1.0
|
C2D
|
A:HEM901
|
4.3
|
22.1
|
1.0
|
C2B
|
A:HEM901
|
4.3
|
10.7
|
1.0
|
C3C
|
A:HEM901
|
4.3
|
19.9
|
1.0
|
C3D
|
A:HEM901
|
4.3
|
17.8
|
1.0
|
C2C
|
A:HEM901
|
4.3
|
17.3
|
1.0
|
CA
|
A:GLY139
|
4.3
|
18.8
|
1.0
|
ND1
|
A:HIS20
|
4.3
|
24.6
|
1.0
|
C2A
|
A:HEM901
|
4.3
|
14.6
|
1.0
|
CG
|
A:HIS20
|
4.3
|
22.8
|
1.0
|
CA
|
A:GLY135
|
4.6
|
15.2
|
1.0
|
O
|
A:GLY135
|
4.9
|
13.3
|
1.0
|
O
|
A:HOH5064
|
4.9
|
15.8
|
1.0
|
CB
|
A:SER138
|
5.0
|
17.9
|
1.0
|
|
Iron binding site 2 out
of 3 in 1v8x
Go back to
Iron Binding Sites List in 1v8x
Iron binding site 2 out
of 3 in the Crystal Structure of the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae
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 the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe902
b:21.9
occ:1.00
|
FE
|
B:HEM902
|
0.0
|
21.9
|
1.0
|
O1
|
B:OXY5002
|
2.0
|
26.2
|
1.0
|
ND
|
B:HEM902
|
2.0
|
24.5
|
1.0
|
NB
|
B:HEM902
|
2.0
|
18.8
|
1.0
|
NA
|
B:HEM902
|
2.0
|
17.8
|
1.0
|
NC
|
B:HEM902
|
2.1
|
24.5
|
1.0
|
NE2
|
B:HIS320
|
2.1
|
23.4
|
1.0
|
O2
|
B:OXY5002
|
2.6
|
32.5
|
1.0
|
C4B
|
B:HEM902
|
3.0
|
21.9
|
1.0
|
C4D
|
B:HEM902
|
3.0
|
21.8
|
1.0
|
C1D
|
B:HEM902
|
3.0
|
23.8
|
1.0
|
C1A
|
B:HEM902
|
3.0
|
18.1
|
1.0
|
CD2
|
B:HIS320
|
3.1
|
20.8
|
1.0
|
C1B
|
B:HEM902
|
3.1
|
16.8
|
1.0
|
C1C
|
B:HEM902
|
3.1
|
25.9
|
1.0
|
C4A
|
B:HEM902
|
3.1
|
17.1
|
1.0
|
CE1
|
B:HIS320
|
3.2
|
23.9
|
1.0
|
C4C
|
B:HEM902
|
3.2
|
29.4
|
1.0
|
CHA
|
B:HEM902
|
3.4
|
20.9
|
1.0
|
CHC
|
B:HEM902
|
3.4
|
22.2
|
1.0
|
CHB
|
B:HEM902
|
3.5
|
16.3
|
1.0
|
CHD
|
B:HEM902
|
3.5
|
30.2
|
1.0
|
C3B
|
B:HEM902
|
4.2
|
20.4
|
1.0
|
C2B
|
B:HEM902
|
4.2
|
15.6
|
1.0
|
C3D
|
B:HEM902
|
4.2
|
29.1
|
1.0
|
CG
|
B:HIS320
|
4.2
|
23.7
|
1.0
|
C2D
|
B:HEM902
|
4.2
|
28.6
|
1.0
|
ND1
|
B:HIS320
|
4.2
|
26.0
|
1.0
|
C3A
|
B:HEM902
|
4.3
|
16.1
|
1.0
|
C2A
|
B:HEM902
|
4.3
|
19.2
|
1.0
|
CA
|
B:GLY439
|
4.3
|
23.9
|
1.0
|
C2C
|
B:HEM902
|
4.3
|
31.1
|
1.0
|
N
|
B:GLY439
|
4.4
|
22.9
|
1.0
|
C3C
|
B:HEM902
|
4.4
|
30.9
|
1.0
|
CA
|
B:GLY435
|
4.6
|
15.1
|
1.0
|
O
|
B:HOH5083
|
4.6
|
20.5
|
1.0
|
O
|
B:GLY435
|
4.8
|
15.6
|
1.0
|
|
Iron binding site 3 out
of 3 in 1v8x
Go back to
Iron Binding Sites List in 1v8x
Iron binding site 3 out
of 3 in the Crystal Structure of the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae
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 the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe903
b:20.6
occ:1.00
|
FE
|
C:HEM903
|
0.0
|
20.6
|
1.0
|
O1
|
C:OXY5003
|
2.0
|
33.2
|
1.0
|
NA
|
C:HEM903
|
2.0
|
20.1
|
1.0
|
ND
|
C:HEM903
|
2.0
|
19.0
|
1.0
|
NE2
|
C:HIS620
|
2.0
|
24.2
|
1.0
|
NB
|
C:HEM903
|
2.0
|
20.3
|
1.0
|
NC
|
C:HEM903
|
2.1
|
20.4
|
1.0
|
O2
|
C:OXY5003
|
2.5
|
33.7
|
1.0
|
CD2
|
C:HIS620
|
2.9
|
26.5
|
1.0
|
C1D
|
C:HEM903
|
3.0
|
21.7
|
1.0
|
C4A
|
C:HEM903
|
3.0
|
18.7
|
1.0
|
C1B
|
C:HEM903
|
3.0
|
19.6
|
1.0
|
C4B
|
C:HEM903
|
3.1
|
19.8
|
1.0
|
C4D
|
C:HEM903
|
3.1
|
20.2
|
1.0
|
C4C
|
C:HEM903
|
3.1
|
22.0
|
1.0
|
C1A
|
C:HEM903
|
3.1
|
18.0
|
1.0
|
CE1
|
C:HIS620
|
3.1
|
27.0
|
1.0
|
C1C
|
C:HEM903
|
3.2
|
19.4
|
1.0
|
CHB
|
C:HEM903
|
3.4
|
19.4
|
1.0
|
CHD
|
C:HEM903
|
3.4
|
24.4
|
1.0
|
CHC
|
C:HEM903
|
3.5
|
20.9
|
1.0
|
CHA
|
C:HEM903
|
3.5
|
18.1
|
1.0
|
CG
|
C:HIS620
|
4.1
|
29.2
|
1.0
|
ND1
|
C:HIS620
|
4.2
|
28.9
|
1.0
|
C3A
|
C:HEM903
|
4.2
|
19.2
|
1.0
|
C2D
|
C:HEM903
|
4.2
|
23.3
|
1.0
|
C2B
|
C:HEM903
|
4.2
|
17.6
|
1.0
|
C3B
|
C:HEM903
|
4.3
|
22.0
|
1.0
|
C2A
|
C:HEM903
|
4.3
|
19.1
|
1.0
|
C3D
|
C:HEM903
|
4.3
|
22.2
|
1.0
|
C3C
|
C:HEM903
|
4.4
|
25.6
|
1.0
|
CA
|
C:GLY735
|
4.4
|
19.3
|
1.0
|
C2C
|
C:HEM903
|
4.4
|
25.2
|
1.0
|
O
|
C:HOH218
|
4.5
|
22.3
|
1.0
|
O
|
C:GLY735
|
4.7
|
19.9
|
1.0
|
C
|
C:GLY735
|
5.0
|
19.1
|
1.0
|
|
Reference:
M.Unno,
T.Matsui,
G.C.Chu,
M.Couture,
T.Yoshida,
D.L.Rousseau,
J.S.Olson,
M.Ikeda-Saito.
Crystal Structure of the Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae: Implications For Heme Oxygenase Function. J.Biol.Chem. V. 279 21055 2004.
ISSN: ISSN 0021-9258
PubMed: 14966119
DOI: 10.1074/JBC.M400491200
Page generated: Sat Aug 3 16:10:45 2024
|