Potassium in PDB 6c0h: Lysinoalanine Synthase, Durn, From Duramycin Biosynthesis Bound to 1- DHA6ALA
Protein crystallography data
The structure of Lysinoalanine Synthase, Durn, From Duramycin Biosynthesis Bound to 1- DHA6ALA, PDB code: 6c0h
was solved by
D.P.Cogan,
S.K.Nair,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
75.84 /
1.90
|
Space group
|
P 41 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
39.990,
39.990,
303.353,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19 /
25.1
|
Potassium Binding Sites:
The binding sites of Potassium atom in the Lysinoalanine Synthase, Durn, From Duramycin Biosynthesis Bound to 1- DHA6ALA
(pdb code 6c0h). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the
Lysinoalanine Synthase, Durn, From Duramycin Biosynthesis Bound to 1- DHA6ALA, PDB code: 6c0h:
Jump to Potassium binding site number:
1;
2;
Potassium binding site 1 out
of 2 in 6c0h
Go back to
Potassium Binding Sites List in 6c0h
Potassium binding site 1 out
of 2 in the Lysinoalanine Synthase, Durn, From Duramycin Biosynthesis Bound to 1- DHA6ALA
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Lysinoalanine Synthase, Durn, From Duramycin Biosynthesis Bound to 1- DHA6ALA within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K201
b:27.9
occ:1.00
|
O
|
A:LEU29
|
2.5
|
26.8
|
1.0
|
O
|
B:LEU45
|
2.7
|
27.2
|
1.0
|
O
|
B:LEU43
|
2.8
|
30.8
|
1.0
|
O
|
A:CYS26
|
2.9
|
24.8
|
1.0
|
O
|
B:ALA42
|
2.9
|
24.9
|
1.0
|
O
|
A:SER27
|
2.9
|
28.8
|
1.0
|
C
|
B:LEU43
|
3.4
|
28.0
|
1.0
|
C
|
A:SER27
|
3.5
|
28.4
|
1.0
|
C
|
B:LEU45
|
3.7
|
31.4
|
1.0
|
CA
|
B:LEU43
|
3.7
|
27.2
|
1.0
|
C
|
A:LEU29
|
3.7
|
25.3
|
1.0
|
CA
|
A:SER27
|
3.7
|
25.8
|
1.0
|
N
|
B:LEU45
|
3.8
|
33.1
|
1.0
|
C
|
A:CYS26
|
3.9
|
25.9
|
1.0
|
C
|
B:ALA42
|
3.9
|
26.4
|
1.0
|
N
|
A:LEU29
|
3.9
|
24.0
|
1.0
|
CA
|
B:LEU45
|
4.1
|
34.8
|
1.0
|
CB
|
B:LEU45
|
4.1
|
35.7
|
1.0
|
N
|
B:LEU43
|
4.3
|
25.8
|
1.0
|
N
|
A:SER27
|
4.3
|
25.4
|
1.0
|
N
|
B:ALA44
|
4.3
|
30.1
|
1.0
|
CD
|
A:PRO31
|
4.4
|
34.3
|
1.0
|
N
|
A:LEU28
|
4.4
|
27.1
|
1.0
|
CA
|
A:LEU29
|
4.4
|
25.3
|
1.0
|
N
|
A:PRO31
|
4.4
|
32.4
|
1.0
|
CB
|
B:GLU47
|
4.4
|
30.4
|
1.0
|
C
|
B:ALA44
|
4.4
|
31.8
|
1.0
|
N
|
B:GLU47
|
4.6
|
27.1
|
1.0
|
CA
|
B:GLU47
|
4.7
|
30.1
|
1.0
|
C
|
A:LEU28
|
4.7
|
28.5
|
1.0
|
C
|
A:PRO30
|
4.7
|
28.8
|
1.0
|
N
|
A:PRO30
|
4.7
|
27.9
|
1.0
|
CB
|
A:LEU29
|
4.8
|
21.7
|
1.0
|
C
|
B:HIS46
|
4.8
|
31.7
|
1.0
|
N
|
B:HIS46
|
4.8
|
32.0
|
1.0
|
CG
|
A:PRO31
|
4.9
|
37.5
|
1.0
|
CA
|
B:ALA44
|
4.9
|
31.6
|
1.0
|
CA
|
A:PRO30
|
4.9
|
29.7
|
1.0
|
CA
|
A:PRO31
|
4.9
|
34.9
|
1.0
|
CB
|
A:PRO31
|
5.0
|
36.5
|
1.0
|
CA
|
A:LEU28
|
5.0
|
27.9
|
1.0
|
CB
|
B:LEU43
|
5.0
|
27.0
|
1.0
|
|
Potassium binding site 2 out
of 2 in 6c0h
Go back to
Potassium Binding Sites List in 6c0h
Potassium binding site 2 out
of 2 in the Lysinoalanine Synthase, Durn, From Duramycin Biosynthesis Bound to 1- DHA6ALA
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Lysinoalanine Synthase, Durn, From Duramycin Biosynthesis Bound to 1- DHA6ALA within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K202
b:27.6
occ:1.00
|
O
|
B:LEU29
|
2.6
|
23.8
|
1.0
|
O
|
A:LEU45
|
2.7
|
30.6
|
1.0
|
O
|
B:SER27
|
2.8
|
30.2
|
1.0
|
O
|
B:CYS26
|
2.8
|
24.2
|
1.0
|
O
|
A:ALA42
|
2.9
|
23.6
|
1.0
|
O
|
A:LEU43
|
2.9
|
25.7
|
1.0
|
C
|
B:SER27
|
3.4
|
30.9
|
1.0
|
C
|
A:LEU43
|
3.4
|
28.3
|
1.0
|
CA
|
B:SER27
|
3.6
|
28.7
|
1.0
|
CA
|
A:LEU43
|
3.7
|
27.2
|
1.0
|
C
|
A:LEU45
|
3.7
|
30.3
|
1.0
|
C
|
B:LEU29
|
3.8
|
25.8
|
1.0
|
N
|
A:LEU45
|
3.8
|
29.1
|
1.0
|
C
|
B:CYS26
|
3.9
|
26.1
|
1.0
|
C
|
A:ALA42
|
3.9
|
25.2
|
1.0
|
N
|
B:LEU29
|
4.0
|
23.6
|
1.0
|
CA
|
A:LEU45
|
4.1
|
32.0
|
1.0
|
CB
|
A:LEU45
|
4.1
|
31.7
|
1.0
|
N
|
B:SER27
|
4.3
|
28.3
|
1.0
|
N
|
A:LEU43
|
4.3
|
24.8
|
1.0
|
N
|
B:LEU28
|
4.3
|
29.0
|
1.0
|
N
|
A:ALA44
|
4.4
|
27.4
|
1.0
|
CA
|
B:LEU29
|
4.4
|
25.6
|
1.0
|
C
|
A:ALA44
|
4.4
|
29.1
|
1.0
|
CD
|
B:PRO31
|
4.5
|
31.2
|
1.0
|
N
|
B:PRO31
|
4.5
|
29.6
|
1.0
|
CB
|
A:GLU47
|
4.5
|
32.5
|
1.0
|
N
|
A:GLU47
|
4.7
|
26.9
|
1.0
|
C
|
B:LEU28
|
4.8
|
28.3
|
1.0
|
C
|
B:PRO30
|
4.8
|
28.8
|
1.0
|
CA
|
A:GLU47
|
4.8
|
29.5
|
1.0
|
C
|
A:HIS46
|
4.8
|
27.6
|
1.0
|
CB
|
B:LEU29
|
4.9
|
24.8
|
1.0
|
N
|
B:PRO30
|
4.9
|
27.5
|
1.0
|
N
|
A:HIS46
|
4.9
|
31.4
|
1.0
|
CB
|
B:PRO31
|
4.9
|
29.0
|
1.0
|
CA
|
A:ALA44
|
4.9
|
28.2
|
1.0
|
CB
|
B:SER27
|
4.9
|
33.9
|
1.0
|
CB
|
A:LEU43
|
4.9
|
24.7
|
1.0
|
CA
|
B:PRO31
|
4.9
|
29.8
|
1.0
|
CA
|
B:PRO30
|
5.0
|
29.1
|
1.0
|
CG
|
B:PRO31
|
5.0
|
33.9
|
1.0
|
CA
|
B:LEU28
|
5.0
|
27.4
|
1.0
|
|
Reference:
L.An,
D.P.Cogan,
C.D.Navo,
G.Jimenez-Oses,
S.K.Nair,
W.A.Van Der Donk.
Substrate-Assisted Enzymatic Formation of Lysinoalanine in Duramycin. Nat. Chem. Biol. V. 14 928 2018.
ISSN: ESSN 1552-4469
PubMed: 30177849
DOI: 10.1038/S41589-018-0122-4
Page generated: Mon Aug 12 15:29:18 2024
|