Chlorine in PDB 6g8k: 14-3-3SIGMA in Complex with A S131BETA3S Mutated Yap PS127 Phosphopeptide
Protein crystallography data
The structure of 14-3-3SIGMA in Complex with A S131BETA3S Mutated Yap PS127 Phosphopeptide, PDB code: 6g8k
was solved by
S.A.Andrei,
V.Thijssen,
L.Brunsveld,
C.Ottmann,
L.G.Milroy,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
55.87 /
1.25
|
Space group
|
C 2 2 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
82.260,
111.730,
62.510,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
14.1 /
16
|
Other elements in 6g8k:
The structure of 14-3-3SIGMA in Complex with A S131BETA3S Mutated Yap PS127 Phosphopeptide also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the 14-3-3SIGMA in Complex with A S131BETA3S Mutated Yap PS127 Phosphopeptide
(pdb code 6g8k). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the
14-3-3SIGMA in Complex with A S131BETA3S Mutated Yap PS127 Phosphopeptide, PDB code: 6g8k:
Jump to Chlorine binding site number:
1;
2;
Chlorine binding site 1 out
of 2 in 6g8k
Go back to
Chlorine Binding Sites List in 6g8k
Chlorine binding site 1 out
of 2 in the 14-3-3SIGMA in Complex with A S131BETA3S Mutated Yap PS127 Phosphopeptide
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 1 of 14-3-3SIGMA in Complex with A S131BETA3S Mutated Yap PS127 Phosphopeptide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl301
b:13.9
occ:1.00
|
O
|
A:HOH729
|
3.0
|
23.4
|
1.0
|
HD2
|
A:LYS87
|
3.0
|
22.1
|
0.4
|
HA
|
A:TYR84
|
3.1
|
12.4
|
1.0
|
O
|
A:HOH670
|
3.1
|
18.9
|
1.0
|
HD2
|
A:LYS87
|
3.2
|
21.4
|
0.6
|
HD1
|
A:TYR84
|
3.2
|
13.1
|
1.0
|
HB2
|
A:LYS87
|
3.4
|
16.8
|
0.4
|
HB2
|
A:LYS87
|
3.4
|
16.2
|
0.6
|
HB3
|
A:GLU83
|
3.6
|
12.9
|
1.0
|
HD3
|
A:LYS87
|
3.7
|
21.4
|
0.6
|
HB2
|
A:TYR84
|
3.8
|
12.4
|
1.0
|
CD
|
A:LYS87
|
3.8
|
18.4
|
0.4
|
CD
|
A:LYS87
|
3.8
|
17.8
|
0.6
|
CA
|
A:TYR84
|
3.8
|
10.4
|
1.0
|
HD3
|
A:LYS87
|
3.8
|
22.1
|
0.4
|
O
|
A:GLU83
|
3.9
|
10.5
|
1.0
|
HB3
|
A:LYS87
|
3.9
|
16.2
|
0.6
|
HB3
|
A:LYS87
|
4.0
|
16.8
|
0.4
|
N
|
A:TYR84
|
4.0
|
10.0
|
1.0
|
CB
|
A:LYS87
|
4.1
|
13.5
|
0.6
|
CB
|
A:LYS87
|
4.1
|
14.0
|
0.4
|
CD1
|
A:TYR84
|
4.1
|
10.9
|
1.0
|
C
|
A:GLU83
|
4.1
|
10.3
|
1.0
|
CB
|
A:TYR84
|
4.2
|
10.3
|
1.0
|
CB
|
A:GLU83
|
4.3
|
10.7
|
1.0
|
HB2
|
A:GLU83
|
4.4
|
12.9
|
1.0
|
HZ3
|
A:LYS87
|
4.4
|
26.3
|
0.4
|
CG
|
A:LYS87
|
4.5
|
16.3
|
0.4
|
H
|
A:TYR84
|
4.5
|
12.0
|
1.0
|
CG
|
A:LYS87
|
4.5
|
15.6
|
0.6
|
O
|
A:HOH511
|
4.5
|
19.2
|
1.0
|
CG
|
A:TYR84
|
4.6
|
10.3
|
1.0
|
HG3
|
A:LYS87
|
4.7
|
19.5
|
0.4
|
HZ1
|
A:LYS87
|
4.8
|
26.3
|
0.4
|
HG3
|
A:LYS87
|
4.8
|
18.8
|
0.6
|
CA
|
A:GLU83
|
4.9
|
10.6
|
1.0
|
H
|
A:LYS87
|
4.9
|
14.4
|
0.6
|
H
|
A:LYS87
|
4.9
|
14.4
|
0.4
|
NZ
|
A:LYS87
|
4.9
|
21.9
|
0.4
|
O
|
A:HOH749
|
4.9
|
41.0
|
1.0
|
CE
|
A:LYS87
|
4.9
|
20.5
|
0.4
|
|
Chlorine binding site 2 out
of 2 in 6g8k
Go back to
Chlorine Binding Sites List in 6g8k
Chlorine binding site 2 out
of 2 in the 14-3-3SIGMA in Complex with A S131BETA3S Mutated Yap PS127 Phosphopeptide
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 2 of 14-3-3SIGMA in Complex with A S131BETA3S Mutated Yap PS127 Phosphopeptide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl302
b:14.1
occ:0.47
|
HH12
|
A:ARG148
|
2.0
|
11.5
|
0.5
|
HG
|
A:SER186
|
2.1
|
15.3
|
1.0
|
HD1
|
A:HIS180
|
2.2
|
12.8
|
1.0
|
NH1
|
A:ARG148
|
2.8
|
9.6
|
0.5
|
O
|
A:HOH722
|
2.8
|
19.8
|
1.0
|
ND1
|
A:HIS180
|
2.8
|
10.7
|
1.0
|
OG
|
A:SER186
|
2.9
|
12.8
|
1.0
|
HB2
|
A:SER186
|
3.0
|
14.6
|
1.0
|
HH11
|
A:ARG148
|
3.1
|
11.5
|
0.5
|
HB1
|
A:ALA184
|
3.1
|
15.9
|
1.0
|
HE1
|
A:HIS180
|
3.2
|
13.1
|
1.0
|
CB
|
A:SER186
|
3.3
|
12.2
|
1.0
|
HB3
|
A:ALA184
|
3.3
|
15.9
|
1.0
|
CE1
|
A:HIS180
|
3.3
|
10.9
|
1.0
|
HB3
|
A:SER186
|
3.4
|
14.6
|
1.0
|
HH22
|
A:ARG148
|
3.6
|
17.1
|
0.5
|
CB
|
A:ALA184
|
3.6
|
13.3
|
1.0
|
HG2
|
A:GLU189
|
3.7
|
12.7
|
1.0
|
CZ
|
A:ARG148
|
3.9
|
12.5
|
0.5
|
HA
|
A:HIS180
|
4.0
|
11.4
|
1.0
|
CG
|
A:HIS180
|
4.0
|
10.1
|
1.0
|
HB2
|
A:ALA184
|
4.0
|
15.9
|
1.0
|
HB3
|
A:GLU189
|
4.1
|
12.0
|
1.0
|
NH2
|
A:ARG148
|
4.1
|
14.2
|
0.5
|
O
|
A:HOH599
|
4.1
|
17.2
|
1.0
|
HE2
|
A:PHE179
|
4.2
|
13.1
|
1.0
|
HB3
|
A:HIS180
|
4.3
|
11.8
|
1.0
|
O
|
A:HOH503
|
4.5
|
15.5
|
1.0
|
O
|
A:HOH709
|
4.5
|
34.9
|
1.0
|
HB2
|
A:GLU189
|
4.5
|
12.0
|
1.0
|
CG
|
A:GLU189
|
4.5
|
10.6
|
1.0
|
CB
|
A:HIS180
|
4.5
|
9.9
|
1.0
|
NE2
|
A:HIS180
|
4.6
|
10.9
|
1.0
|
CB
|
A:GLU189
|
4.6
|
10.0
|
1.0
|
O
|
A:ALA184
|
4.7
|
14.0
|
1.0
|
O
|
A:HOH645
|
4.7
|
44.9
|
1.0
|
CA
|
A:HIS180
|
4.7
|
9.5
|
1.0
|
CA
|
A:SER186
|
4.8
|
11.3
|
1.0
|
CD2
|
A:HIS180
|
4.9
|
10.5
|
1.0
|
CE2
|
A:PHE179
|
4.9
|
10.9
|
1.0
|
HH21
|
A:ARG148
|
5.0
|
17.1
|
0.5
|
CA
|
A:ALA184
|
5.0
|
12.5
|
1.0
|
|
Reference:
S.A.Andrei,
V.Thijssen,
L.Brunsveld,
C.Ottmann,
L.G.Milroy.
A Study on the Effect of Synthetic Alpha-to-BETA3-Amino Acid Mutations on the Binding of Phosphopeptides to 14-3-3 Proteins. Chem.Commun.(Camb.) 2019.
ISSN: ESSN 1364-548X
PubMed: 31763628
DOI: 10.1039/C9CC07982C
Page generated: Sat Dec 12 13:01:01 2020
|