Potassium in PDB 4tlz: Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn
Protein crystallography data
The structure of Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn, PDB code: 4tlz
was solved by
J.W.Setser,
C.L.Drennan,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
47.30 /
2.41
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
84.620,
157.660,
165.293,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
17.8 /
21.5
|
Potassium Binding Sites:
The binding sites of Potassium atom in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn
(pdb code 4tlz). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 8 binding sites of Potassium where determined in the
Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn, PDB code: 4tlz:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Potassium binding site 1 out
of 8 in 4tlz
Go back to
Potassium Binding Sites List in 4tlz
Potassium binding site 1 out
of 8 in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K504
b:48.2
occ:1.00
|
O
|
A:SER33
|
2.7
|
28.2
|
1.0
|
O
|
A:LEU30
|
3.0
|
24.7
|
1.0
|
O
|
A:ALA35
|
3.3
|
38.2
|
1.0
|
O
|
A:GLU31
|
3.4
|
27.3
|
1.0
|
O
|
A:HOH736
|
3.6
|
29.1
|
1.0
|
C
|
A:SER33
|
3.9
|
28.6
|
1.0
|
C
|
A:GLU31
|
3.9
|
24.8
|
1.0
|
CA
|
A:GLU31
|
4.0
|
23.9
|
1.0
|
C
|
A:LEU30
|
4.0
|
23.1
|
1.0
|
C
|
A:ALA35
|
4.4
|
38.5
|
1.0
|
N
|
A:SER33
|
4.5
|
27.7
|
1.0
|
N
|
A:GLU31
|
4.5
|
23.8
|
1.0
|
CA
|
A:SER33
|
4.6
|
26.4
|
1.0
|
C
|
A:PRO34
|
4.7
|
30.7
|
1.0
|
O
|
A:PRO34
|
4.7
|
34.4
|
1.0
|
N
|
A:GLU32
|
4.8
|
25.7
|
1.0
|
N
|
A:PRO34
|
4.9
|
24.5
|
1.0
|
CB
|
A:SER33
|
4.9
|
25.9
|
1.0
|
CA
|
A:PRO34
|
5.0
|
32.5
|
1.0
|
N
|
A:ALA35
|
5.0
|
30.7
|
1.0
|
C
|
A:GLU32
|
5.0
|
27.0
|
1.0
|
|
Potassium binding site 2 out
of 8 in 4tlz
Go back to
Potassium Binding Sites List in 4tlz
Potassium binding site 2 out
of 8 in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K505
b:40.0
occ:1.00
|
O
|
A:LEU118
|
2.8
|
34.2
|
1.0
|
O
|
A:GLU115
|
2.8
|
31.2
|
1.0
|
O
|
A:HOH650
|
2.9
|
36.5
|
1.0
|
O
|
A:HIS120
|
3.0
|
40.8
|
1.0
|
O
|
A:SER116
|
3.6
|
31.9
|
1.0
|
OE1
|
A:GLU121
|
3.8
|
55.3
|
1.0
|
C
|
A:LEU118
|
3.8
|
33.0
|
1.0
|
K
|
A:K506
|
3.9
|
79.0
|
1.0
|
C
|
A:GLU115
|
3.9
|
27.7
|
1.0
|
CB
|
A:LEU118
|
4.0
|
29.2
|
1.0
|
C
|
A:HIS120
|
4.1
|
33.6
|
1.0
|
C
|
A:SER116
|
4.1
|
24.3
|
1.0
|
CA
|
A:SER116
|
4.2
|
30.7
|
1.0
|
CA
|
A:LEU118
|
4.3
|
32.2
|
1.0
|
CD
|
A:GLU121
|
4.3
|
56.0
|
1.0
|
OE2
|
A:GLU115
|
4.4
|
41.4
|
1.0
|
O
|
A:ALA119
|
4.4
|
36.6
|
1.0
|
N
|
A:LEU118
|
4.4
|
26.0
|
1.0
|
CA
|
A:GLU121
|
4.5
|
30.2
|
1.0
|
N
|
A:SER116
|
4.5
|
25.0
|
1.0
|
CD
|
A:GLU115
|
4.5
|
33.5
|
1.0
|
OE2
|
A:GLU121
|
4.6
|
60.5
|
1.0
|
C
|
A:ALA119
|
4.6
|
32.5
|
1.0
|
OE1
|
A:GLU115
|
4.6
|
31.8
|
1.0
|
N
|
A:GLU121
|
4.7
|
33.8
|
1.0
|
N
|
A:ALA119
|
4.9
|
31.3
|
1.0
|
CG
|
A:LEU118
|
4.9
|
31.9
|
1.0
|
N
|
A:HIS120
|
5.0
|
32.6
|
1.0
|
|
Potassium binding site 3 out
of 8 in 4tlz
Go back to
Potassium Binding Sites List in 4tlz
Potassium binding site 3 out
of 8 in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K506
b:79.0
occ:1.00
|
O
|
A:SER116
|
2.6
|
31.9
|
1.0
|
O
|
A:LEU118
|
2.9
|
34.2
|
1.0
|
C
|
A:LEU118
|
3.8
|
33.0
|
1.0
|
C
|
A:SER116
|
3.8
|
24.3
|
1.0
|
K
|
A:K505
|
3.9
|
40.0
|
1.0
|
O
|
A:LYS117
|
4.0
|
29.5
|
1.0
|
C
|
A:LYS117
|
4.1
|
26.8
|
1.0
|
CA
|
A:ALA119
|
4.4
|
31.8
|
1.0
|
N
|
A:ALA119
|
4.5
|
31.3
|
1.0
|
N
|
A:LEU118
|
4.5
|
26.0
|
1.0
|
O
|
A:ALA119
|
4.5
|
36.6
|
1.0
|
CA
|
A:LYS117
|
4.5
|
25.0
|
1.0
|
N
|
A:LYS117
|
4.6
|
24.5
|
1.0
|
CA
|
A:LEU118
|
4.8
|
32.2
|
1.0
|
C
|
A:ALA119
|
4.8
|
32.5
|
1.0
|
CA
|
A:SER116
|
4.9
|
30.7
|
1.0
|
|
Potassium binding site 4 out
of 8 in 4tlz
Go back to
Potassium Binding Sites List in 4tlz
Potassium binding site 4 out
of 8 in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K504
b:47.1
occ:1.00
|
O
|
B:SER33
|
2.6
|
34.7
|
1.0
|
O
|
B:LEU30
|
2.8
|
23.4
|
1.0
|
O
|
B:ALA35
|
3.1
|
36.1
|
1.0
|
O
|
B:GLU31
|
3.4
|
26.3
|
1.0
|
C
|
B:SER33
|
3.7
|
28.3
|
1.0
|
C
|
B:GLU31
|
3.9
|
24.9
|
1.0
|
C
|
B:LEU30
|
3.9
|
19.4
|
1.0
|
CA
|
B:GLU31
|
4.0
|
21.3
|
1.0
|
C
|
B:ALA35
|
4.2
|
36.6
|
1.0
|
N
|
B:SER33
|
4.3
|
24.5
|
1.0
|
N
|
B:GLU31
|
4.4
|
20.2
|
1.0
|
CA
|
B:SER33
|
4.5
|
25.7
|
1.0
|
C
|
B:PRO34
|
4.6
|
37.8
|
1.0
|
O
|
B:PRO34
|
4.6
|
40.8
|
1.0
|
CB
|
B:SER33
|
4.6
|
26.4
|
1.0
|
N
|
B:PRO34
|
4.7
|
29.8
|
1.0
|
N
|
B:GLU32
|
4.8
|
23.8
|
1.0
|
N
|
B:ALA35
|
4.8
|
32.4
|
1.0
|
CA
|
B:PRO34
|
4.9
|
35.1
|
1.0
|
C
|
B:GLU32
|
4.9
|
24.5
|
1.0
|
|
Potassium binding site 5 out
of 8 in 4tlz
Go back to
Potassium Binding Sites List in 4tlz
Potassium binding site 5 out
of 8 in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 5 of Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K505
b:55.9
occ:1.00
|
O
|
B:HOH610
|
2.9
|
49.5
|
1.0
|
O
|
B:LEU118
|
3.0
|
39.0
|
1.0
|
O
|
B:GLU115
|
3.0
|
30.5
|
1.0
|
O
|
B:HOH703
|
3.1
|
37.3
|
1.0
|
O
|
B:HIS120
|
3.4
|
46.7
|
1.0
|
O
|
B:SER116
|
3.5
|
37.2
|
1.0
|
CA
|
B:SER116
|
4.0
|
25.0
|
1.0
|
C
|
B:SER116
|
4.0
|
27.9
|
1.0
|
C
|
B:GLU115
|
4.0
|
30.4
|
1.0
|
CG
|
B:GLU121
|
4.1
|
55.3
|
1.0
|
C
|
B:LEU118
|
4.1
|
33.3
|
1.0
|
OE2
|
B:GLU115
|
4.3
|
40.9
|
1.0
|
CB
|
B:LEU118
|
4.4
|
31.1
|
1.0
|
N
|
B:SER116
|
4.5
|
26.6
|
1.0
|
C
|
B:HIS120
|
4.5
|
37.7
|
1.0
|
CD
|
B:GLU115
|
4.5
|
39.2
|
1.0
|
OE1
|
B:GLU115
|
4.6
|
37.9
|
1.0
|
OE1
|
B:GLU121
|
4.6
|
75.8
|
1.0
|
N
|
B:LEU118
|
4.6
|
29.2
|
1.0
|
CA
|
B:LEU118
|
4.6
|
30.6
|
1.0
|
O
|
B:ALA119
|
4.6
|
55.0
|
1.0
|
CA
|
B:GLU121
|
4.7
|
38.8
|
1.0
|
CD
|
B:GLU121
|
4.9
|
64.9
|
1.0
|
C
|
B:ALA119
|
5.0
|
46.6
|
1.0
|
|
Potassium binding site 6 out
of 8 in 4tlz
Go back to
Potassium Binding Sites List in 4tlz
Potassium binding site 6 out
of 8 in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 6 of Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K504
b:64.8
occ:1.00
|
O
|
C:SER33
|
2.9
|
48.1
|
1.0
|
O
|
C:LEU30
|
3.0
|
41.5
|
1.0
|
O
|
C:GLU31
|
3.4
|
38.2
|
1.0
|
O
|
C:ALA35
|
3.4
|
62.6
|
1.0
|
C
|
C:GLU31
|
3.9
|
35.7
|
1.0
|
CA
|
C:GLU31
|
4.0
|
33.7
|
1.0
|
C
|
C:SER33
|
4.1
|
50.4
|
1.0
|
C
|
C:LEU30
|
4.1
|
40.0
|
1.0
|
N
|
C:GLU31
|
4.5
|
37.6
|
1.0
|
C
|
C:ALA35
|
4.5
|
62.0
|
1.0
|
N
|
C:SER33
|
4.6
|
33.1
|
1.0
|
O
|
C:PRO34
|
4.8
|
62.0
|
1.0
|
CA
|
C:SER33
|
4.8
|
48.3
|
1.0
|
C
|
C:PRO34
|
4.8
|
59.8
|
1.0
|
N
|
C:GLU32
|
4.9
|
34.9
|
1.0
|
|
Potassium binding site 7 out
of 8 in 4tlz
Go back to
Potassium Binding Sites List in 4tlz
Potassium binding site 7 out
of 8 in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 7 of Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K505
b:60.0
occ:1.00
|
O
|
C:HIS120
|
3.0
|
60.5
|
1.0
|
O
|
C:GLU115
|
3.0
|
40.6
|
1.0
|
O
|
C:LEU118
|
3.0
|
45.9
|
1.0
|
O
|
C:HOH714
|
3.5
|
42.4
|
1.0
|
OE1
|
C:GLU121
|
3.5
|
72.6
|
1.0
|
O
|
C:SER116
|
3.8
|
47.9
|
1.0
|
CD
|
C:GLU121
|
4.0
|
71.9
|
1.0
|
C
|
C:LEU118
|
4.0
|
46.8
|
1.0
|
C
|
C:HIS120
|
4.1
|
52.9
|
1.0
|
C
|
C:GLU115
|
4.1
|
41.9
|
1.0
|
OE2
|
C:GLU115
|
4.2
|
50.1
|
1.0
|
CA
|
C:SER116
|
4.3
|
37.5
|
1.0
|
C
|
C:SER116
|
4.3
|
42.1
|
1.0
|
OE2
|
C:GLU121
|
4.3
|
74.4
|
1.0
|
CB
|
C:LEU118
|
4.3
|
41.2
|
1.0
|
CA
|
C:GLU121
|
4.3
|
48.2
|
1.0
|
CD
|
C:GLU115
|
4.4
|
43.8
|
1.0
|
O
|
C:ALA119
|
4.5
|
43.6
|
1.0
|
OE1
|
C:GLU115
|
4.6
|
43.1
|
1.0
|
CA
|
C:LEU118
|
4.6
|
39.3
|
1.0
|
N
|
C:SER116
|
4.6
|
38.2
|
1.0
|
N
|
C:GLU121
|
4.7
|
49.3
|
1.0
|
N
|
C:LEU118
|
4.7
|
36.7
|
1.0
|
C
|
C:ALA119
|
4.8
|
49.6
|
1.0
|
|
Potassium binding site 8 out
of 8 in 4tlz
Go back to
Potassium Binding Sites List in 4tlz
Potassium binding site 8 out
of 8 in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 8 of Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:K504
b:54.3
occ:1.00
|
O
|
D:SER33
|
2.8
|
37.8
|
1.0
|
O
|
D:LEU30
|
3.0
|
32.8
|
1.0
|
O
|
D:GLU31
|
3.3
|
34.0
|
1.0
|
O
|
D:ALA35
|
3.4
|
48.2
|
1.0
|
C
|
D:GLU31
|
3.8
|
33.5
|
1.0
|
CA
|
D:GLU31
|
3.9
|
30.4
|
1.0
|
C
|
D:SER33
|
4.0
|
35.2
|
1.0
|
C
|
D:LEU30
|
4.0
|
29.9
|
1.0
|
N
|
D:GLU31
|
4.5
|
30.2
|
1.0
|
C
|
D:ALA35
|
4.5
|
44.6
|
1.0
|
N
|
D:SER33
|
4.5
|
34.1
|
1.0
|
CA
|
D:SER33
|
4.7
|
33.1
|
1.0
|
O
|
D:PRO34
|
4.8
|
41.8
|
1.0
|
C
|
D:PRO34
|
4.8
|
43.1
|
1.0
|
N
|
D:GLU32
|
4.8
|
34.8
|
1.0
|
N
|
D:PRO34
|
5.0
|
42.8
|
1.0
|
CB
|
D:SER33
|
5.0
|
32.7
|
1.0
|
|
Reference:
J.W.Setser,
J.R.Heemstra,
C.T.Walsh,
C.L.Drennan.
Crystallographic Evidence For Drastic Conformational Changes in the Active Site of A Flavin-Dependent N-Hydroxylase. Biochemistry 2014.
ISSN: ISSN 0006-2960
PubMed: 25184411
DOI: 10.1021/BI500655Q
Page generated: Mon Aug 12 12:06:36 2024
|