Iron in PDB 4u9g: Crystal Structure of An H-Nox Protein From S. Oneidensis in the Fe(II)Co Ligation State, Q154A/Q155A/K156A Mutant
Protein crystallography data
The structure of Crystal Structure of An H-Nox Protein From S. Oneidensis in the Fe(II)Co Ligation State, Q154A/Q155A/K156A Mutant, PDB code: 4u9g
was solved by
M.A.Herzik Jr.,
R.Jonnalagadda,
J.Kuriyan,
M.A.Marletta,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
43.01 /
2.25
|
Space group
|
P 63 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
164.173,
164.173,
102.366,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
18.2 /
19.3
|
Other elements in 4u9g:
The structure of Crystal Structure of An H-Nox Protein From S. Oneidensis in the Fe(II)Co Ligation State, Q154A/Q155A/K156A Mutant also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of An H-Nox Protein From S. Oneidensis in the Fe(II)Co Ligation State, Q154A/Q155A/K156A Mutant
(pdb code 4u9g). 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 An H-Nox Protein From S. Oneidensis in the Fe(II)Co Ligation State, Q154A/Q155A/K156A Mutant, PDB code: 4u9g:
Jump to Iron binding site number:
1;
2;
Iron binding site 1 out
of 2 in 4u9g
Go back to
Iron Binding Sites List in 4u9g
Iron binding site 1 out
of 2 in the Crystal Structure of An H-Nox Protein From S. Oneidensis in the Fe(II)Co Ligation State, Q154A/Q155A/K156A Mutant
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 An H-Nox Protein From S. Oneidensis in the Fe(II)Co Ligation State, Q154A/Q155A/K156A Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe201
b:39.7
occ:1.00
|
FE
|
A:HEM201
|
0.0
|
39.7
|
1.0
|
C
|
A:CMO203
|
1.9
|
58.7
|
1.0
|
NB
|
A:HEM201
|
2.0
|
40.0
|
1.0
|
NC
|
A:HEM201
|
2.1
|
42.0
|
1.0
|
NA
|
A:HEM201
|
2.1
|
38.8
|
1.0
|
ND
|
A:HEM201
|
2.2
|
39.4
|
1.0
|
NE2
|
A:HIS103
|
2.2
|
36.2
|
1.0
|
C1B
|
A:HEM201
|
3.0
|
37.9
|
1.0
|
C4A
|
A:HEM201
|
3.0
|
38.2
|
1.0
|
CE1
|
A:HIS103
|
3.1
|
41.7
|
1.0
|
C4C
|
A:HEM201
|
3.1
|
41.2
|
1.0
|
C4B
|
A:HEM201
|
3.1
|
39.7
|
1.0
|
O
|
A:CMO203
|
3.1
|
67.3
|
1.0
|
C1D
|
A:HEM201
|
3.1
|
42.4
|
1.0
|
C1C
|
A:HEM201
|
3.1
|
41.5
|
1.0
|
C1A
|
A:HEM201
|
3.2
|
39.0
|
1.0
|
HE1
|
A:HIS103
|
3.2
|
50.0
|
1.0
|
C4D
|
A:HEM201
|
3.2
|
41.8
|
1.0
|
CD2
|
A:HIS103
|
3.3
|
42.0
|
1.0
|
CHB
|
A:HEM201
|
3.4
|
37.6
|
1.0
|
CHD
|
A:HEM201
|
3.4
|
41.3
|
1.0
|
HD2
|
A:HIS103
|
3.5
|
50.4
|
1.0
|
CHC
|
A:HEM201
|
3.5
|
40.4
|
1.0
|
CHA
|
A:HEM201
|
3.6
|
38.8
|
1.0
|
C3A
|
A:HEM201
|
4.2
|
39.8
|
1.0
|
ND1
|
A:HIS103
|
4.3
|
39.3
|
1.0
|
C2B
|
A:HEM201
|
4.3
|
38.4
|
1.0
|
C2A
|
A:HEM201
|
4.3
|
39.4
|
1.0
|
C3B
|
A:HEM201
|
4.3
|
40.4
|
1.0
|
HHB
|
A:HEM201
|
4.3
|
45.2
|
1.0
|
C3C
|
A:HEM201
|
4.3
|
44.6
|
1.0
|
C2C
|
A:HEM201
|
4.3
|
42.6
|
1.0
|
C2D
|
A:HEM201
|
4.4
|
42.3
|
1.0
|
CG
|
A:HIS103
|
4.4
|
43.0
|
1.0
|
C3D
|
A:HEM201
|
4.4
|
40.9
|
1.0
|
HD13
|
A:LEU145
|
4.4
|
46.9
|
1.0
|
HHD
|
A:HEM201
|
4.4
|
49.6
|
1.0
|
HD22
|
A:LEU115
|
4.4
|
53.0
|
1.0
|
HHC
|
A:HEM201
|
4.5
|
48.5
|
1.0
|
HHA
|
A:HEM201
|
4.5
|
46.6
|
1.0
|
HD13
|
A:LEU77
|
4.6
|
48.7
|
1.0
|
HD23
|
A:LEU115
|
4.7
|
53.0
|
1.0
|
HD22
|
A:LEU145
|
4.8
|
46.9
|
1.0
|
HD21
|
A:LEU115
|
4.9
|
53.0
|
1.0
|
CD2
|
A:LEU115
|
4.9
|
44.1
|
1.0
|
HG23
|
A:ILE98
|
4.9
|
49.4
|
1.0
|
HG22
|
A:ILE102
|
5.0
|
47.6
|
1.0
|
|
Iron binding site 2 out
of 2 in 4u9g
Go back to
Iron Binding Sites List in 4u9g
Iron binding site 2 out
of 2 in the Crystal Structure of An H-Nox Protein From S. Oneidensis in the Fe(II)Co Ligation State, Q154A/Q155A/K156A Mutant
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 An H-Nox Protein From S. Oneidensis in the Fe(II)Co Ligation State, Q154A/Q155A/K156A Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe201
b:53.8
occ:1.00
|
FE
|
B:HEM201
|
0.0
|
53.8
|
1.0
|
NB
|
B:HEM201
|
2.0
|
52.7
|
1.0
|
NA
|
B:HEM201
|
2.1
|
47.8
|
1.0
|
NC
|
B:HEM201
|
2.1
|
57.4
|
1.0
|
ND
|
B:HEM201
|
2.1
|
51.5
|
1.0
|
NE2
|
B:HIS103
|
2.4
|
63.0
|
1.0
|
C1B
|
B:HEM201
|
3.0
|
51.3
|
1.0
|
C4A
|
B:HEM201
|
3.0
|
47.9
|
1.0
|
C4B
|
B:HEM201
|
3.1
|
55.5
|
1.0
|
C1D
|
B:HEM201
|
3.1
|
57.3
|
1.0
|
C1C
|
B:HEM201
|
3.1
|
56.8
|
1.0
|
C1A
|
B:HEM201
|
3.1
|
46.0
|
1.0
|
C4D
|
B:HEM201
|
3.1
|
51.7
|
1.0
|
C4C
|
B:HEM201
|
3.1
|
56.7
|
1.0
|
CE1
|
B:HIS103
|
3.2
|
59.6
|
1.0
|
HE1
|
B:HIS103
|
3.3
|
71.6
|
1.0
|
CHB
|
B:HEM201
|
3.4
|
46.9
|
1.0
|
CHD
|
B:HEM201
|
3.4
|
58.9
|
1.0
|
CD2
|
B:HIS103
|
3.4
|
67.4
|
1.0
|
CHC
|
B:HEM201
|
3.5
|
55.4
|
1.0
|
CHA
|
B:HEM201
|
3.5
|
46.5
|
1.0
|
HD2
|
B:HIS103
|
3.6
|
80.9
|
1.0
|
HD13
|
B:LEU145
|
3.8
|
68.3
|
1.0
|
HD13
|
B:LEU77
|
4.0
|
74.8
|
1.0
|
HHB
|
B:HEM201
|
4.2
|
56.3
|
1.0
|
C3A
|
B:HEM201
|
4.3
|
48.2
|
1.0
|
HD11
|
B:LEU77
|
4.3
|
74.8
|
1.0
|
C2B
|
B:HEM201
|
4.3
|
50.1
|
1.0
|
C3B
|
B:HEM201
|
4.3
|
56.0
|
1.0
|
C2A
|
B:HEM201
|
4.3
|
42.1
|
1.0
|
C2C
|
B:HEM201
|
4.3
|
59.4
|
1.0
|
C2D
|
B:HEM201
|
4.3
|
53.5
|
1.0
|
C3C
|
B:HEM201
|
4.3
|
58.4
|
1.0
|
C3D
|
B:HEM201
|
4.3
|
49.0
|
1.0
|
HHD
|
B:HEM201
|
4.4
|
70.7
|
1.0
|
ND1
|
B:HIS103
|
4.4
|
62.5
|
1.0
|
HHC
|
B:HEM201
|
4.4
|
66.5
|
1.0
|
HHA
|
B:HEM201
|
4.4
|
55.8
|
1.0
|
CD1
|
B:LEU77
|
4.5
|
62.4
|
1.0
|
HD22
|
B:LEU115
|
4.5
|
71.9
|
1.0
|
HD11
|
B:LEU145
|
4.5
|
68.3
|
1.0
|
CG
|
B:HIS103
|
4.5
|
64.0
|
1.0
|
CD1
|
B:LEU145
|
4.6
|
56.9
|
1.0
|
HD12
|
B:LEU77
|
4.7
|
74.8
|
1.0
|
HD23
|
B:LEU115
|
4.9
|
71.9
|
1.0
|
HD22
|
B:LEU145
|
4.9
|
67.9
|
1.0
|
HG23
|
B:ILE98
|
5.0
|
73.7
|
1.0
|
|
Reference:
M.A.Herzik,
R.Jonnalagadda,
J.Kuriyan,
M.A.Marletta.
Structural Insights Into the Role of Iron-Histidine Bond Cleavage in Nitric Oxide-Induced Activation of H-Nox Gas Sensor Proteins. Proc.Natl.Acad.Sci.Usa V. 111 E4156 2014.
ISSN: ESSN 1091-6490
PubMed: 25253889
DOI: 10.1073/PNAS.1416936111
Page generated: Mon Aug 5 11:57:08 2024
|