Iron in PDB 1t3q: Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86
Enzymatic activity of Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86
All present enzymatic activity of Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86:
1.3.99.17;
Protein crystallography data
The structure of Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86, PDB code: 1t3q
was solved by
I.Bonin,
B.M.Martins,
V.Purvanov,
S.Fetzner,
R.Huber,
H.Dobbek,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
19.29 /
1.80
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
278.320,
72.100,
202.650,
90.00,
127.98,
90.00
|
R / Rfree (%)
|
18.6 /
20.7
|
Other elements in 1t3q:
The structure of Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86 also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86
(pdb code 1t3q). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the
Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86, PDB code: 1t3q:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Iron binding site 1 out
of 8 in 1t3q
Go back to
Iron Binding Sites List in 1t3q
Iron binding site 1 out
of 8 in the Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86
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 Quinoline 2-Oxidoreductase From Pseudomonas Putida 86 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe4907
b:14.9
occ:1.00
|
FE1
|
A:FES4907
|
0.0
|
14.9
|
1.0
|
S2
|
A:FES4907
|
2.2
|
18.6
|
1.0
|
S1
|
A:FES4907
|
2.3
|
15.3
|
1.0
|
SG
|
A:CYS107
|
2.3
|
16.9
|
1.0
|
SG
|
A:CYS144
|
2.4
|
15.5
|
1.0
|
FE2
|
A:FES4907
|
2.7
|
16.3
|
1.0
|
CB
|
A:CYS144
|
3.2
|
17.1
|
1.0
|
CB
|
A:CYS107
|
3.4
|
15.7
|
1.0
|
N
|
A:CYS107
|
3.6
|
12.8
|
1.0
|
N
|
A:GLY108
|
3.8
|
12.7
|
1.0
|
O
|
B:HOH4927
|
3.9
|
17.2
|
1.0
|
CA
|
A:CYS107
|
3.9
|
14.2
|
1.0
|
N
|
A:CYS144
|
4.1
|
16.2
|
1.0
|
C
|
A:CYS107
|
4.3
|
13.6
|
1.0
|
N
|
A:PHE109
|
4.3
|
14.5
|
1.0
|
CA
|
A:CYS144
|
4.3
|
17.2
|
1.0
|
SG
|
A:CYS142
|
4.4
|
17.9
|
1.0
|
C
|
A:GLN106
|
4.7
|
12.6
|
1.0
|
SG
|
A:CYS110
|
4.7
|
15.1
|
1.0
|
CA
|
A:GLY108
|
4.7
|
14.3
|
1.0
|
CB
|
A:GLN106
|
4.8
|
14.4
|
1.0
|
N
|
A:ARG143
|
4.8
|
15.3
|
1.0
|
N
|
A:GLN106
|
4.9
|
14.3
|
1.0
|
N
|
A:CYS110
|
4.9
|
14.5
|
1.0
|
CB
|
A:PHE109
|
4.9
|
16.4
|
1.0
|
C
|
A:GLY108
|
5.0
|
14.4
|
1.0
|
|
Iron binding site 2 out
of 8 in 1t3q
Go back to
Iron Binding Sites List in 1t3q
Iron binding site 2 out
of 8 in the Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86
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 Quinoline 2-Oxidoreductase From Pseudomonas Putida 86 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe4907
b:16.3
occ:1.00
|
FE2
|
A:FES4907
|
0.0
|
16.3
|
1.0
|
S1
|
A:FES4907
|
2.2
|
15.3
|
1.0
|
S2
|
A:FES4907
|
2.2
|
18.6
|
1.0
|
SG
|
A:CYS110
|
2.3
|
15.1
|
1.0
|
SG
|
A:CYS142
|
2.4
|
17.9
|
1.0
|
FE1
|
A:FES4907
|
2.7
|
14.9
|
1.0
|
CB
|
A:CYS142
|
3.4
|
15.4
|
1.0
|
CB
|
A:CYS110
|
3.4
|
14.3
|
1.0
|
CA
|
A:CYS142
|
3.7
|
15.3
|
1.0
|
N
|
A:CYS110
|
4.1
|
14.5
|
1.0
|
N
|
A:ARG143
|
4.2
|
15.3
|
1.0
|
CB
|
A:CYS144
|
4.3
|
17.1
|
1.0
|
C
|
A:CYS142
|
4.4
|
13.7
|
1.0
|
CA
|
A:CYS110
|
4.4
|
14.8
|
1.0
|
N
|
A:CYS144
|
4.4
|
16.2
|
1.0
|
O
|
A:HOH4914
|
4.6
|
14.8
|
1.0
|
SG
|
A:CYS144
|
4.6
|
15.5
|
1.0
|
CG2
|
A:THR145
|
4.6
|
14.9
|
1.0
|
SG
|
A:CYS107
|
4.7
|
16.9
|
1.0
|
O
|
A:LEU141
|
4.9
|
16.2
|
1.0
|
CA
|
A:CYS144
|
4.9
|
17.2
|
1.0
|
N
|
A:CYS142
|
5.0
|
16.8
|
1.0
|
N
|
A:PHE109
|
5.0
|
14.5
|
1.0
|
|
Iron binding site 3 out
of 8 in 1t3q
Go back to
Iron Binding Sites List in 1t3q
Iron binding site 3 out
of 8 in the Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86
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 Quinoline 2-Oxidoreductase From Pseudomonas Putida 86 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe4908
b:16.1
occ:1.00
|
FE1
|
A:FES4908
|
0.0
|
16.1
|
1.0
|
S2
|
A:FES4908
|
2.2
|
17.3
|
1.0
|
S1
|
A:FES4908
|
2.3
|
18.3
|
1.0
|
SG
|
A:CYS53
|
2.3
|
16.8
|
1.0
|
SG
|
A:CYS48
|
2.4
|
18.0
|
1.0
|
FE2
|
A:FES4908
|
2.7
|
17.1
|
1.0
|
N
|
A:CYS48
|
3.5
|
17.6
|
1.0
|
CB
|
A:CYS53
|
3.6
|
17.1
|
1.0
|
N
|
A:CYS53
|
3.6
|
15.9
|
1.0
|
CB
|
A:CYS48
|
3.6
|
16.8
|
1.0
|
N
|
A:GLY54
|
3.7
|
14.6
|
1.0
|
N
|
A:GLU49
|
3.7
|
18.4
|
1.0
|
CA
|
A:CYS53
|
3.9
|
16.9
|
1.0
|
CA
|
A:CYS48
|
3.9
|
17.8
|
1.0
|
OG
|
A:SER55
|
4.2
|
23.5
|
1.0
|
C
|
A:CYS53
|
4.2
|
16.1
|
1.0
|
N
|
A:GLY47
|
4.2
|
15.9
|
1.0
|
C
|
A:GLY47
|
4.3
|
19.4
|
1.0
|
C
|
A:CYS48
|
4.3
|
19.0
|
1.0
|
N
|
A:SER55
|
4.3
|
14.6
|
1.0
|
N
|
A:VAL52
|
4.4
|
16.6
|
1.0
|
N
|
A:GLY51
|
4.4
|
19.0
|
1.0
|
SG
|
A:CYS68
|
4.5
|
17.4
|
1.0
|
CA
|
A:GLY47
|
4.6
|
18.7
|
1.0
|
C
|
A:VAL52
|
4.6
|
17.8
|
1.0
|
N
|
A:GLN50
|
4.6
|
19.4
|
1.0
|
CA
|
A:GLU49
|
4.7
|
20.1
|
1.0
|
SG
|
A:CYS56
|
4.7
|
15.0
|
1.0
|
CA
|
A:GLY54
|
4.7
|
13.9
|
1.0
|
C
|
A:GLY51
|
4.7
|
19.4
|
1.0
|
CA
|
A:GLY51
|
4.8
|
19.3
|
1.0
|
C
|
A:GLY54
|
5.0
|
14.4
|
1.0
|
N
|
A:CYS56
|
5.0
|
14.8
|
1.0
|
|
Iron binding site 4 out
of 8 in 1t3q
Go back to
Iron Binding Sites List in 1t3q
Iron binding site 4 out
of 8 in the Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86
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 Quinoline 2-Oxidoreductase From Pseudomonas Putida 86 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe4908
b:17.1
occ:1.00
|
FE2
|
A:FES4908
|
0.0
|
17.1
|
1.0
|
S1
|
A:FES4908
|
2.1
|
18.3
|
1.0
|
S2
|
A:FES4908
|
2.3
|
17.3
|
1.0
|
SG
|
A:CYS56
|
2.3
|
15.0
|
1.0
|
SG
|
A:CYS68
|
2.4
|
17.4
|
1.0
|
FE1
|
A:FES4908
|
2.7
|
16.1
|
1.0
|
CB
|
A:CYS68
|
3.2
|
16.9
|
1.0
|
CB
|
A:CYS56
|
3.4
|
13.9
|
1.0
|
N
|
A:CYS56
|
4.2
|
14.8
|
1.0
|
N
|
A:CYS68
|
4.3
|
17.3
|
1.0
|
N
|
A:GLY51
|
4.3
|
19.0
|
1.0
|
CA
|
A:CYS68
|
4.4
|
18.3
|
1.0
|
N
|
A:GLU49
|
4.4
|
18.4
|
1.0
|
CA
|
A:GLY51
|
4.4
|
19.3
|
1.0
|
CA
|
A:CYS56
|
4.4
|
13.9
|
1.0
|
SG
|
A:CYS48
|
4.4
|
18.0
|
1.0
|
CB
|
A:ARG66
|
4.6
|
15.7
|
1.0
|
CA
|
A:GLU49
|
4.6
|
20.1
|
1.0
|
CD
|
A:ARG66
|
4.6
|
17.8
|
1.0
|
SG
|
A:CYS53
|
4.7
|
16.8
|
1.0
|
N
|
A:GLY54
|
4.8
|
14.6
|
1.0
|
N
|
A:GLN50
|
4.9
|
19.4
|
1.0
|
|
Iron binding site 5 out
of 8 in 1t3q
Go back to
Iron Binding Sites List in 1t3q
Iron binding site 5 out
of 8 in the Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe4909
b:16.7
occ:1.00
|
FE1
|
D:FES4909
|
0.0
|
16.7
|
1.0
|
S1
|
D:FES4909
|
2.2
|
17.2
|
1.0
|
S2
|
D:FES4909
|
2.2
|
16.7
|
1.0
|
SG
|
D:CYS107
|
2.4
|
16.6
|
1.0
|
SG
|
D:CYS144
|
2.5
|
18.8
|
1.0
|
FE2
|
D:FES4909
|
2.6
|
17.0
|
1.0
|
CB
|
D:CYS144
|
3.3
|
19.6
|
1.0
|
CB
|
D:CYS107
|
3.4
|
13.6
|
1.0
|
N
|
D:CYS107
|
3.6
|
15.7
|
1.0
|
N
|
D:GLY108
|
3.8
|
16.4
|
1.0
|
CA
|
D:CYS107
|
3.9
|
16.2
|
1.0
|
O
|
E:HOH4932
|
4.0
|
15.7
|
1.0
|
N
|
D:CYS144
|
4.0
|
18.9
|
1.0
|
C
|
D:CYS107
|
4.3
|
16.5
|
1.0
|
N
|
D:PHE109
|
4.3
|
15.5
|
1.0
|
SG
|
D:CYS142
|
4.3
|
17.4
|
1.0
|
CA
|
D:CYS144
|
4.3
|
18.5
|
1.0
|
N
|
D:ARG143
|
4.7
|
17.6
|
1.0
|
SG
|
D:CYS110
|
4.7
|
18.4
|
1.0
|
C
|
D:GLN106
|
4.8
|
14.9
|
1.0
|
CA
|
D:GLY108
|
4.8
|
15.4
|
1.0
|
N
|
D:CYS110
|
4.9
|
18.0
|
1.0
|
N
|
D:GLN106
|
4.9
|
14.8
|
1.0
|
CB
|
D:PHE109
|
4.9
|
15.9
|
1.0
|
C
|
D:ARG143
|
4.9
|
18.1
|
1.0
|
CB
|
D:GLN106
|
4.9
|
16.7
|
1.0
|
C
|
D:GLY108
|
5.0
|
16.3
|
1.0
|
|
Iron binding site 6 out
of 8 in 1t3q
Go back to
Iron Binding Sites List in 1t3q
Iron binding site 6 out
of 8 in the Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe4909
b:17.0
occ:1.00
|
FE2
|
D:FES4909
|
0.0
|
17.0
|
1.0
|
S1
|
D:FES4909
|
2.2
|
17.2
|
1.0
|
S2
|
D:FES4909
|
2.2
|
16.7
|
1.0
|
SG
|
D:CYS110
|
2.3
|
18.4
|
1.0
|
SG
|
D:CYS142
|
2.4
|
17.4
|
1.0
|
FE1
|
D:FES4909
|
2.6
|
16.7
|
1.0
|
CB
|
D:CYS142
|
3.4
|
14.2
|
1.0
|
CB
|
D:CYS110
|
3.4
|
17.2
|
1.0
|
CA
|
D:CYS142
|
3.7
|
14.8
|
1.0
|
N
|
D:CYS110
|
4.0
|
18.0
|
1.0
|
N
|
D:ARG143
|
4.1
|
17.6
|
1.0
|
CA
|
D:CYS110
|
4.3
|
16.2
|
1.0
|
C
|
D:CYS142
|
4.4
|
15.9
|
1.0
|
N
|
D:CYS144
|
4.4
|
18.9
|
1.0
|
O
|
D:HOH4918
|
4.5
|
15.5
|
1.0
|
CB
|
D:CYS144
|
4.5
|
19.6
|
1.0
|
SG
|
D:CYS144
|
4.6
|
18.8
|
1.0
|
SG
|
D:CYS107
|
4.6
|
16.6
|
1.0
|
CG2
|
D:THR145
|
4.9
|
16.7
|
1.0
|
N
|
D:PHE109
|
4.9
|
15.5
|
1.0
|
O
|
D:LEU141
|
4.9
|
18.2
|
1.0
|
C
|
D:CYS110
|
5.0
|
17.4
|
1.0
|
N
|
D:GLY108
|
5.0
|
16.4
|
1.0
|
|
Iron binding site 7 out
of 8 in 1t3q
Go back to
Iron Binding Sites List in 1t3q
Iron binding site 7 out
of 8 in the Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe4910
b:16.8
occ:1.00
|
FE1
|
D:FES4910
|
0.0
|
16.8
|
1.0
|
S2
|
D:FES4910
|
2.2
|
14.7
|
1.0
|
S1
|
D:FES4910
|
2.2
|
15.3
|
1.0
|
SG
|
D:CYS53
|
2.3
|
17.3
|
1.0
|
SG
|
D:CYS48
|
2.4
|
18.2
|
1.0
|
FE2
|
D:FES4910
|
2.8
|
17.1
|
1.0
|
N
|
D:CYS48
|
3.5
|
18.8
|
1.0
|
CB
|
D:CYS53
|
3.5
|
14.6
|
1.0
|
N
|
D:CYS53
|
3.5
|
18.1
|
1.0
|
CB
|
D:CYS48
|
3.6
|
16.7
|
1.0
|
N
|
D:GLY54
|
3.7
|
16.7
|
1.0
|
N
|
D:GLU49
|
3.8
|
20.5
|
1.0
|
CA
|
D:CYS53
|
3.9
|
16.4
|
1.0
|
CA
|
D:CYS48
|
3.9
|
18.6
|
1.0
|
OG
|
D:SER55
|
4.1
|
23.8
|
1.0
|
C
|
D:CYS53
|
4.2
|
18.1
|
1.0
|
N
|
D:GLY47
|
4.2
|
18.9
|
1.0
|
C
|
D:GLY47
|
4.2
|
19.8
|
1.0
|
N
|
D:SER55
|
4.3
|
17.1
|
1.0
|
C
|
D:CYS48
|
4.3
|
19.4
|
1.0
|
N
|
D:VAL52
|
4.3
|
18.1
|
1.0
|
N
|
D:GLY51
|
4.4
|
21.1
|
1.0
|
CA
|
D:GLY47
|
4.5
|
18.5
|
1.0
|
SG
|
D:CYS68
|
4.5
|
17.5
|
1.0
|
C
|
D:VAL52
|
4.6
|
18.7
|
1.0
|
N
|
D:GLN50
|
4.7
|
19.5
|
1.0
|
CA
|
D:GLY54
|
4.7
|
16.2
|
1.0
|
SG
|
D:CYS56
|
4.7
|
17.3
|
1.0
|
C
|
D:GLY51
|
4.7
|
19.6
|
1.0
|
CA
|
D:GLY51
|
4.7
|
19.4
|
1.0
|
CA
|
D:GLU49
|
4.8
|
20.8
|
1.0
|
C
|
D:GLY54
|
4.9
|
15.9
|
1.0
|
CB
|
D:SER55
|
4.9
|
19.7
|
1.0
|
N
|
D:CYS56
|
5.0
|
15.2
|
1.0
|
CA
|
D:VAL52
|
5.0
|
18.8
|
1.0
|
|
Iron binding site 8 out
of 8 in 1t3q
Go back to
Iron Binding Sites List in 1t3q
Iron binding site 8 out
of 8 in the Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe4910
b:17.1
occ:1.00
|
FE2
|
D:FES4910
|
0.0
|
17.1
|
1.0
|
S1
|
D:FES4910
|
2.2
|
15.3
|
1.0
|
S2
|
D:FES4910
|
2.3
|
14.7
|
1.0
|
SG
|
D:CYS56
|
2.4
|
17.3
|
1.0
|
SG
|
D:CYS68
|
2.4
|
17.5
|
1.0
|
FE1
|
D:FES4910
|
2.8
|
16.8
|
1.0
|
CB
|
D:CYS68
|
3.2
|
16.3
|
1.0
|
CB
|
D:CYS56
|
3.4
|
15.7
|
1.0
|
N
|
D:CYS68
|
4.2
|
17.6
|
1.0
|
N
|
D:GLY51
|
4.2
|
21.1
|
1.0
|
N
|
D:CYS56
|
4.3
|
15.2
|
1.0
|
CA
|
D:CYS68
|
4.3
|
17.8
|
1.0
|
CA
|
D:GLY51
|
4.3
|
19.4
|
1.0
|
N
|
D:GLU49
|
4.4
|
20.5
|
1.0
|
SG
|
D:CYS48
|
4.4
|
18.2
|
1.0
|
CA
|
D:CYS56
|
4.4
|
15.3
|
1.0
|
CA
|
D:GLU49
|
4.6
|
20.8
|
1.0
|
CB
|
D:ARG66
|
4.6
|
18.4
|
1.0
|
CD
|
D:ARG66
|
4.7
|
19.4
|
1.0
|
SG
|
D:CYS53
|
4.8
|
17.3
|
1.0
|
N
|
D:GLN50
|
4.9
|
19.5
|
1.0
|
N
|
D:GLY54
|
4.9
|
16.7
|
1.0
|
OG
|
D:SER55
|
5.0
|
23.8
|
1.0
|
|
Reference:
I.Bonin,
B.M.Martins,
V.Purvanov,
S.Fetzner,
R.Huber,
H.Dobbek.
Active Site Geometry and Substrate Recognition of the Molybdenum Hydroxylase Quinoline 2-Oxidoreductase. Structure V. 12 1425 2004.
ISSN: ISSN 0969-2126
PubMed: 15296736
DOI: 10.1016/J.STR.2004.05.014
Page generated: Sat Aug 3 15:08:17 2024
|