Iron in PDB 2q0j: Structure of Pseudomonas Quinolone Signal Response Protein Pqse
Protein crystallography data
The structure of Structure of Pseudomonas Quinolone Signal Response Protein Pqse, PDB code: 2q0j
was solved by
S.Yu,
V.Jensen,
I.Feldmann,
S.Haussler,
W.Blankenfeldt,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
19.82 /
2.10
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
44.760,
66.090,
110.260,
90.00,
97.19,
90.00
|
R / Rfree (%)
|
15.1 /
21.1
|
Iron Binding Sites:
The binding sites of Iron atom in the Structure of Pseudomonas Quinolone Signal Response Protein Pqse
(pdb code 2q0j). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the
Structure of Pseudomonas Quinolone Signal Response Protein Pqse, PDB code: 2q0j:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 2q0j
Go back to
Iron Binding Sites List in 2q0j
Iron binding site 1 out
of 4 in the Structure of Pseudomonas Quinolone Signal Response Protein Pqse
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Structure of Pseudomonas Quinolone Signal Response Protein Pqse within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe997
b:23.8
occ:1.00
|
O
|
A:HOH999
|
1.9
|
27.5
|
1.0
|
ND1
|
A:HIS71
|
2.2
|
19.8
|
1.0
|
NE2
|
A:HIS159
|
2.2
|
19.6
|
1.0
|
NE2
|
A:HIS69
|
2.2
|
19.7
|
1.0
|
OD2
|
A:ASP178
|
2.5
|
22.9
|
1.0
|
CD2
|
A:HIS69
|
3.1
|
24.2
|
1.0
|
CE1
|
A:HIS71
|
3.1
|
19.9
|
1.0
|
CD2
|
A:HIS159
|
3.1
|
19.5
|
1.0
|
CE1
|
A:HIS159
|
3.2
|
20.0
|
1.0
|
CG
|
A:HIS71
|
3.2
|
19.3
|
1.0
|
CE1
|
A:HIS69
|
3.2
|
17.8
|
1.0
|
CG
|
A:ASP178
|
3.5
|
20.6
|
1.0
|
CB
|
A:HIS71
|
3.6
|
18.9
|
1.0
|
O2
|
A:BEZ500
|
3.6
|
26.9
|
0.7
|
FE
|
A:FE998
|
3.8
|
21.7
|
1.0
|
CD2
|
A:HIS74
|
3.8
|
17.9
|
1.0
|
CB
|
A:ASP178
|
3.9
|
18.8
|
1.0
|
NE2
|
A:HIS74
|
3.9
|
17.2
|
1.0
|
O1
|
A:BEZ500
|
4.2
|
22.3
|
0.7
|
NE2
|
A:HIS71
|
4.2
|
21.9
|
1.0
|
CG
|
A:HIS159
|
4.3
|
19.1
|
1.0
|
OD1
|
A:ASP73
|
4.3
|
18.4
|
1.0
|
CG
|
A:HIS69
|
4.3
|
18.9
|
1.0
|
C
|
A:BEZ500
|
4.3
|
25.7
|
0.7
|
ND1
|
A:HIS159
|
4.3
|
18.4
|
1.0
|
ND1
|
A:HIS69
|
4.3
|
18.7
|
1.0
|
CD2
|
A:HIS71
|
4.3
|
19.1
|
1.0
|
OD1
|
A:ASP178
|
4.7
|
20.0
|
1.0
|
CG
|
A:HIS74
|
4.8
|
17.0
|
1.0
|
CE1
|
A:HIS74
|
5.0
|
17.0
|
1.0
|
OD2
|
A:ASP73
|
5.0
|
18.8
|
1.0
|
|
Iron binding site 2 out
of 4 in 2q0j
Go back to
Iron Binding Sites List in 2q0j
Iron binding site 2 out
of 4 in the Structure of Pseudomonas Quinolone Signal Response Protein Pqse
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Structure of Pseudomonas Quinolone Signal Response Protein Pqse within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe998
b:21.7
occ:1.00
|
O1
|
A:BEZ500
|
2.0
|
22.3
|
0.7
|
NE2
|
A:HIS221
|
2.1
|
18.0
|
1.0
|
NE2
|
A:HIS74
|
2.1
|
17.2
|
1.0
|
OD2
|
A:ASP178
|
2.2
|
22.9
|
1.0
|
OD2
|
A:ASP73
|
2.4
|
18.8
|
1.0
|
O
|
A:HOH999
|
2.7
|
27.5
|
1.0
|
CG
|
A:ASP178
|
3.0
|
20.6
|
1.0
|
CE1
|
A:HIS74
|
3.0
|
17.0
|
1.0
|
OD1
|
A:ASP178
|
3.1
|
20.0
|
1.0
|
CE1
|
A:HIS221
|
3.1
|
17.7
|
1.0
|
CD2
|
A:HIS221
|
3.1
|
19.8
|
1.0
|
C
|
A:BEZ500
|
3.1
|
25.7
|
0.7
|
CD2
|
A:HIS74
|
3.2
|
17.9
|
1.0
|
CG
|
A:ASP73
|
3.3
|
16.2
|
1.0
|
O2
|
A:BEZ500
|
3.6
|
26.9
|
0.7
|
OD1
|
A:ASP73
|
3.6
|
18.4
|
1.0
|
FE
|
A:FE997
|
3.8
|
23.8
|
1.0
|
ND1
|
A:HIS74
|
4.2
|
20.0
|
1.0
|
ND1
|
A:HIS221
|
4.2
|
18.6
|
1.0
|
CG
|
A:HIS221
|
4.2
|
18.1
|
1.0
|
CG
|
A:HIS74
|
4.3
|
17.0
|
1.0
|
C1
|
A:BEZ500
|
4.4
|
26.2
|
0.7
|
CB
|
A:ASP178
|
4.4
|
18.8
|
1.0
|
CB
|
A:ASP73
|
4.6
|
17.9
|
1.0
|
C2
|
A:BEZ500
|
4.6
|
25.7
|
0.7
|
NE2
|
A:HIS69
|
4.7
|
19.7
|
1.0
|
CE1
|
A:HIS69
|
4.7
|
17.8
|
1.0
|
|
Iron binding site 3 out
of 4 in 2q0j
Go back to
Iron Binding Sites List in 2q0j
Iron binding site 3 out
of 4 in the Structure of Pseudomonas Quinolone Signal Response Protein Pqse
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Structure of Pseudomonas Quinolone Signal Response Protein Pqse within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe997
b:27.3
occ:1.00
|
O
|
B:HOH999
|
1.9
|
30.6
|
1.0
|
ND1
|
B:HIS71
|
2.1
|
24.3
|
1.0
|
NE2
|
B:HIS69
|
2.2
|
19.4
|
1.0
|
NE2
|
B:HIS159
|
2.2
|
18.4
|
1.0
|
OD2
|
B:ASP178
|
2.7
|
25.2
|
1.0
|
CE1
|
B:HIS71
|
3.0
|
25.8
|
1.0
|
CD2
|
B:HIS69
|
3.1
|
23.4
|
1.0
|
CD2
|
B:HIS159
|
3.1
|
18.5
|
1.0
|
CE1
|
B:HIS159
|
3.2
|
20.4
|
1.0
|
CG
|
B:HIS71
|
3.2
|
27.5
|
1.0
|
CE1
|
B:HIS69
|
3.2
|
23.9
|
1.0
|
O2
|
B:BEZ500
|
3.4
|
30.0
|
0.7
|
CB
|
B:HIS71
|
3.5
|
25.9
|
1.0
|
FE
|
B:FE998
|
3.7
|
26.4
|
1.0
|
CG
|
B:ASP178
|
3.7
|
23.2
|
1.0
|
CD2
|
B:HIS74
|
3.8
|
23.0
|
1.0
|
NE2
|
B:HIS74
|
3.8
|
22.8
|
1.0
|
CB
|
B:ASP178
|
3.9
|
21.1
|
1.0
|
O1
|
B:BEZ500
|
4.1
|
30.0
|
0.7
|
NE2
|
B:HIS71
|
4.2
|
24.4
|
1.0
|
C
|
B:BEZ500
|
4.2
|
30.2
|
0.7
|
ND1
|
B:HIS159
|
4.3
|
19.8
|
1.0
|
CD2
|
B:HIS71
|
4.3
|
27.1
|
1.0
|
CG
|
B:HIS159
|
4.3
|
19.5
|
1.0
|
ND1
|
B:HIS69
|
4.3
|
23.5
|
1.0
|
CG
|
B:HIS69
|
4.3
|
23.0
|
1.0
|
OD1
|
B:ASP73
|
4.4
|
27.2
|
1.0
|
OD1
|
B:ASP178
|
4.8
|
25.3
|
1.0
|
CG
|
B:HIS74
|
4.8
|
23.4
|
1.0
|
CE1
|
B:HIS74
|
4.9
|
25.6
|
1.0
|
OD2
|
B:ASP73
|
4.9
|
28.7
|
1.0
|
CA
|
B:HIS71
|
5.0
|
25.9
|
1.0
|
|
Iron binding site 4 out
of 4 in 2q0j
Go back to
Iron Binding Sites List in 2q0j
Iron binding site 4 out
of 4 in the Structure of Pseudomonas Quinolone Signal Response Protein Pqse
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Structure of Pseudomonas Quinolone Signal Response Protein Pqse within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe998
b:26.4
occ:1.00
|
O1
|
B:BEZ500
|
1.9
|
30.0
|
0.7
|
NE2
|
B:HIS74
|
2.1
|
22.8
|
1.0
|
OD2
|
B:ASP178
|
2.1
|
25.2
|
1.0
|
NE2
|
B:HIS221
|
2.1
|
24.1
|
1.0
|
O
|
B:HOH999
|
2.4
|
30.6
|
1.0
|
OD2
|
B:ASP73
|
2.4
|
28.7
|
1.0
|
CG
|
B:ASP178
|
3.0
|
23.2
|
1.0
|
CE1
|
B:HIS221
|
3.0
|
24.8
|
1.0
|
CE1
|
B:HIS74
|
3.1
|
25.6
|
1.0
|
CD2
|
B:HIS74
|
3.1
|
23.0
|
1.0
|
C
|
B:BEZ500
|
3.1
|
30.2
|
0.7
|
OD1
|
B:ASP178
|
3.1
|
25.3
|
1.0
|
CD2
|
B:HIS221
|
3.2
|
24.6
|
1.0
|
CG
|
B:ASP73
|
3.3
|
25.5
|
1.0
|
O2
|
B:BEZ500
|
3.5
|
30.0
|
0.7
|
FE
|
B:FE997
|
3.7
|
27.3
|
1.0
|
OD1
|
B:ASP73
|
3.7
|
27.2
|
1.0
|
ND1
|
B:HIS74
|
4.2
|
22.7
|
1.0
|
CG
|
B:HIS74
|
4.2
|
23.4
|
1.0
|
ND1
|
B:HIS221
|
4.2
|
24.5
|
1.0
|
C1
|
B:BEZ500
|
4.3
|
28.9
|
0.7
|
CG
|
B:HIS221
|
4.3
|
23.7
|
1.0
|
CB
|
B:ASP178
|
4.4
|
21.1
|
1.0
|
C2
|
B:BEZ500
|
4.5
|
29.4
|
0.7
|
CE1
|
B:HIS69
|
4.6
|
23.9
|
1.0
|
CB
|
B:ASP73
|
4.6
|
26.2
|
1.0
|
NE2
|
B:HIS69
|
4.6
|
19.4
|
1.0
|
|
Reference:
S.Yu,
V.Jensen,
J.Seeliger,
I.Feldmann,
S.Weber,
E.Schleicher,
S.Haussler,
W.Blankenfeldt.
Structure Elucidation and Preliminary Assessment of Hydrolase Activity of Pqse, the Pseudomonas Quinolone Signal (Pqs) Response Protein. Biochemistry V. 48 10298 2009.
ISSN: ISSN 0006-2960
PubMed: 19788310
DOI: 10.1021/BI900123J
Page generated: Sun Aug 4 01:35:25 2024
|