Iron in PDB 4gph: Structure of Hmuo, Heme Oxygenase From Corynebacterium Diphtheriae, in Complex with the Putative Reaction Intermediates Between FE3+- Biliverdin and Biliverdin (Data Set IV)
Enzymatic activity of Structure of Hmuo, Heme Oxygenase From Corynebacterium Diphtheriae, in Complex with the Putative Reaction Intermediates Between FE3+- Biliverdin and Biliverdin (Data Set IV)
All present enzymatic activity of Structure of Hmuo, Heme Oxygenase From Corynebacterium Diphtheriae, in Complex with the Putative Reaction Intermediates Between FE3+- Biliverdin and Biliverdin (Data Set IV):
1.14.99.3;
Protein crystallography data
The structure of Structure of Hmuo, Heme Oxygenase From Corynebacterium Diphtheriae, in Complex with the Putative Reaction Intermediates Between FE3+- Biliverdin and Biliverdin (Data Set IV), PDB code: 4gph
was solved by
M.Unno,
M.Ikeda-Saito,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
30.00 /
1.70
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
54.065,
62.966,
107.728,
90.00,
100.78,
90.00
|
R / Rfree (%)
|
16.5 /
20.5
|
Iron Binding Sites:
The binding sites of Iron atom in the Structure of Hmuo, Heme Oxygenase From Corynebacterium Diphtheriae, in Complex with the Putative Reaction Intermediates Between FE3+- Biliverdin and Biliverdin (Data Set IV)
(pdb code 4gph). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the
Structure of Hmuo, Heme Oxygenase From Corynebacterium Diphtheriae, in Complex with the Putative Reaction Intermediates Between FE3+- Biliverdin and Biliverdin (Data Set IV), PDB code: 4gph:
Jump to Iron binding site number:
1;
2;
Iron binding site 1 out
of 2 in 4gph
Go back to
Iron Binding Sites List in 4gph
Iron binding site 1 out
of 2 in the Structure of Hmuo, Heme Oxygenase From Corynebacterium Diphtheriae, in Complex with the Putative Reaction Intermediates Between FE3+- Biliverdin and Biliverdin (Data Set IV)
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Structure of Hmuo, Heme Oxygenase From Corynebacterium Diphtheriae, in Complex with the Putative Reaction Intermediates Between FE3+- Biliverdin and Biliverdin (Data Set IV) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe3001
b:49.1
occ:0.30
|
NA
|
A:BLA3002
|
1.6
|
27.8
|
0.3
|
NA
|
A:BLA3002
|
1.6
|
37.3
|
0.7
|
NB
|
A:BLA3002
|
2.0
|
25.2
|
0.3
|
O
|
A:HOH3161
|
2.2
|
16.4
|
0.3
|
NB
|
A:BLA3002
|
2.2
|
40.5
|
0.7
|
ND
|
A:BLA3002
|
2.2
|
63.8
|
0.7
|
ND
|
A:BLA3002
|
2.3
|
56.2
|
0.3
|
NC
|
A:BLA3002
|
2.3
|
58.7
|
0.3
|
C4A
|
A:BLA3002
|
2.6
|
22.4
|
0.3
|
C1A
|
A:BLA3002
|
2.7
|
41.3
|
0.7
|
NC
|
A:BLA3002
|
2.7
|
63.4
|
0.7
|
C4A
|
A:BLA3002
|
2.7
|
33.8
|
0.7
|
C1B
|
A:BLA3002
|
2.7
|
21.0
|
0.3
|
C1A
|
A:BLA3002
|
2.8
|
31.2
|
0.3
|
C1B
|
A:BLA3002
|
3.0
|
34.5
|
0.7
|
CHB
|
A:BLA3002
|
3.0
|
21.7
|
0.3
|
C4D
|
A:BLA3002
|
3.1
|
66.6
|
0.7
|
CHA
|
A:BLA3002
|
3.1
|
55.6
|
0.7
|
C4B
|
A:BLA3002
|
3.1
|
30.4
|
0.3
|
C4D
|
A:BLA3002
|
3.2
|
59.0
|
0.3
|
CHB
|
A:BLA3002
|
3.2
|
32.7
|
0.7
|
C4B
|
A:BLA3002
|
3.2
|
45.0
|
0.7
|
CHA
|
A:BLA3002
|
3.2
|
46.5
|
0.3
|
C1C
|
A:BLA3002
|
3.3
|
60.7
|
0.3
|
C1D
|
A:BLA3002
|
3.4
|
71.5
|
0.3
|
C4C
|
A:BLA3002
|
3.4
|
71.0
|
0.3
|
C1D
|
A:BLA3002
|
3.4
|
78.2
|
0.7
|
CHD
|
A:BLA3002
|
3.6
|
75.1
|
0.3
|
OB
|
A:BLA3002
|
3.6
|
38.4
|
0.3
|
OB
|
A:BLA3002
|
3.6
|
52.2
|
0.7
|
OC
|
A:BLA3002
|
3.6
|
57.2
|
0.3
|
NE2
|
A:HIS20
|
3.7
|
43.5
|
1.0
|
C4C
|
A:BLA3002
|
3.7
|
76.6
|
0.7
|
CHD
|
A:BLA3002
|
3.7
|
80.6
|
0.7
|
C1C
|
A:BLA3002
|
3.7
|
65.7
|
0.7
|
C3A
|
A:BLA3002
|
3.9
|
21.4
|
0.3
|
C2A
|
A:BLA3002
|
3.9
|
39.8
|
0.7
|
C2A
|
A:BLA3002
|
3.9
|
28.0
|
0.3
|
C3A
|
A:BLA3002
|
3.9
|
32.0
|
0.7
|
CE1
|
A:HIS20
|
4.0
|
42.7
|
1.0
|
C2B
|
A:BLA3002
|
4.0
|
23.8
|
0.3
|
OC
|
A:BLA3002
|
4.0
|
62.2
|
0.7
|
C2B
|
A:BLA3002
|
4.1
|
38.5
|
0.7
|
C3B
|
A:BLA3002
|
4.2
|
28.9
|
0.3
|
C3B
|
A:BLA3002
|
4.3
|
44.0
|
0.7
|
O
|
A:HOH3173
|
4.3
|
36.0
|
1.0
|
CA
|
A:GLY135
|
4.3
|
27.9
|
1.0
|
O
|
A:GLY135
|
4.4
|
28.6
|
1.0
|
C3D
|
A:BLA3002
|
4.4
|
85.9
|
0.7
|
C3D
|
A:BLA3002
|
4.5
|
78.7
|
0.3
|
C2D
|
A:BLA3002
|
4.6
|
85.9
|
0.3
|
C2D
|
A:BLA3002
|
4.6
|
93.3
|
0.7
|
C2C
|
A:BLA3002
|
4.6
|
72.4
|
0.3
|
C3C
|
A:BLA3002
|
4.6
|
80.0
|
0.3
|
CD2
|
A:HIS20
|
4.8
|
43.5
|
1.0
|
N
|
A:GLY139
|
4.8
|
39.2
|
1.0
|
C
|
A:GLY135
|
4.8
|
25.8
|
1.0
|
CA
|
A:GLY139
|
4.9
|
41.3
|
1.0
|
C3C
|
A:BLA3002
|
4.9
|
86.1
|
0.7
|
C2C
|
A:BLA3002
|
5.0
|
78.5
|
0.7
|
|
Iron binding site 2 out
of 2 in 4gph
Go back to
Iron Binding Sites List in 4gph
Iron binding site 2 out
of 2 in the Structure of Hmuo, Heme Oxygenase From Corynebacterium Diphtheriae, in Complex with the Putative Reaction Intermediates Between FE3+- Biliverdin and Biliverdin (Data Set IV)
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Structure of Hmuo, Heme Oxygenase From Corynebacterium Diphtheriae, in Complex with the Putative Reaction Intermediates Between FE3+- Biliverdin and Biliverdin (Data Set IV) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe901
b:55.0
occ:0.40
|
NB
|
C:BLA902
|
1.9
|
29.3
|
0.3
|
NA
|
C:BLA902
|
1.9
|
25.1
|
0.3
|
NA
|
C:BLA902
|
1.9
|
29.5
|
0.7
|
NB
|
C:BLA902
|
2.0
|
35.0
|
0.7
|
ND
|
C:BLA902
|
2.0
|
25.1
|
0.3
|
ND
|
C:BLA902
|
2.0
|
27.7
|
0.7
|
NC
|
C:BLA902
|
2.4
|
28.4
|
0.3
|
NC
|
C:BLA902
|
2.5
|
32.2
|
0.7
|
O3
|
C:ASC903
|
2.6
|
29.7
|
1.0
|
C4B
|
C:BLA902
|
2.9
|
31.9
|
0.3
|
C1B
|
C:BLA902
|
2.9
|
30.0
|
0.3
|
C4D
|
C:BLA902
|
2.9
|
26.8
|
0.3
|
C1B
|
C:BLA902
|
2.9
|
36.2
|
0.7
|
C1A
|
C:BLA902
|
2.9
|
27.8
|
0.3
|
C4D
|
C:BLA902
|
2.9
|
30.2
|
0.7
|
C4B
|
C:BLA902
|
3.0
|
38.1
|
0.7
|
C4A
|
C:BLA902
|
3.0
|
33.3
|
0.7
|
C1A
|
C:BLA902
|
3.0
|
31.9
|
0.7
|
C4A
|
C:BLA902
|
3.0
|
28.1
|
0.3
|
C1D
|
C:BLA902
|
3.0
|
27.3
|
0.7
|
C1D
|
C:BLA902
|
3.0
|
25.2
|
0.3
|
CHA
|
C:BLA902
|
3.2
|
27.9
|
0.3
|
OB
|
C:BLA902
|
3.2
|
33.2
|
0.3
|
CHA
|
C:BLA902
|
3.3
|
32.3
|
0.7
|
OB
|
C:BLA902
|
3.3
|
38.3
|
0.7
|
CHB
|
C:BLA902
|
3.3
|
39.5
|
0.7
|
C4C
|
C:BLA902
|
3.3
|
26.3
|
0.3
|
C3
|
C:ASC903
|
3.3
|
37.6
|
1.0
|
CHB
|
C:BLA902
|
3.3
|
31.1
|
0.3
|
CHD
|
C:BLA902
|
3.4
|
26.1
|
0.3
|
C4C
|
C:BLA902
|
3.4
|
27.2
|
0.7
|
CHD
|
C:BLA902
|
3.4
|
28.5
|
0.7
|
C1C
|
C:BLA902
|
3.4
|
29.8
|
0.3
|
C1C
|
C:BLA902
|
3.6
|
32.1
|
0.7
|
OC
|
C:BLA902
|
3.8
|
41.5
|
0.7
|
OC
|
C:BLA902
|
3.9
|
30.6
|
0.3
|
C2
|
C:ASC903
|
4.0
|
32.7
|
1.0
|
CA
|
C:GLY735
|
4.0
|
21.7
|
1.0
|
C3B
|
C:BLA902
|
4.1
|
34.3
|
0.3
|
C2B
|
C:BLA902
|
4.1
|
34.4
|
0.3
|
C3B
|
C:BLA902
|
4.1
|
40.6
|
0.7
|
C2B
|
C:BLA902
|
4.1
|
41.8
|
0.7
|
C3D
|
C:BLA902
|
4.1
|
28.7
|
0.7
|
C3D
|
C:BLA902
|
4.2
|
26.8
|
0.3
|
C3A
|
C:BLA902
|
4.2
|
33.9
|
0.7
|
C2A
|
C:BLA902
|
4.2
|
28.6
|
0.3
|
C2A
|
C:BLA902
|
4.2
|
30.7
|
0.7
|
C3A
|
C:BLA902
|
4.2
|
29.8
|
0.3
|
O2
|
C:ASC903
|
4.2
|
33.7
|
1.0
|
C4
|
C:ASC903
|
4.2
|
39.6
|
1.0
|
C2D
|
C:BLA902
|
4.2
|
27.6
|
0.7
|
C2D
|
C:BLA902
|
4.3
|
25.6
|
0.3
|
NE2
|
C:HIS620
|
4.3
|
33.5
|
1.0
|
O
|
C:GLY735
|
4.3
|
21.9
|
1.0
|
C3C
|
C:BLA902
|
4.5
|
28.3
|
0.3
|
C3C
|
C:BLA902
|
4.6
|
30.1
|
0.7
|
C2C
|
C:BLA902
|
4.6
|
30.0
|
0.3
|
C
|
C:GLY735
|
4.7
|
21.1
|
1.0
|
C2C
|
C:BLA902
|
4.7
|
33.1
|
0.7
|
CB
|
C:SER738
|
4.7
|
22.0
|
1.0
|
CE1
|
C:HIS620
|
4.8
|
31.6
|
1.0
|
N
|
C:GLY739
|
4.9
|
20.2
|
1.0
|
|
Reference:
M.Unno,
A.Ardevol,
C.Rovira,
M.Ikeda-Saito.
Crystal Structures of the Substrate-Free and the Product-Bound Forms of Hmuo, A Heme Oxygenase From Corynebacterium Diphtheriae To Be Published.
Page generated: Mon Aug 5 03:02:26 2024
|