Chlorine in PDB 6g8p: 14-3-3SIGMA in Complex with A P129BETA3P and L132BETA3L Mutated Yap PS127 Phosphopeptide

Protein crystallography data

The structure of 14-3-3SIGMA in Complex with A P129BETA3P and L132BETA3L Mutated Yap PS127 Phosphopeptide, PDB code: 6g8p 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) 41.59 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 82.037, 111.499, 62.460, 90.00, 90.00, 90.00
R / Rfree (%) 13.3 / 15.9

Other elements in 6g8p:

The structure of 14-3-3SIGMA in Complex with A P129BETA3P and L132BETA3L Mutated Yap PS127 Phosphopeptide also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the 14-3-3SIGMA in Complex with A P129BETA3P and L132BETA3L Mutated Yap PS127 Phosphopeptide (pdb code 6g8p). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the 14-3-3SIGMA in Complex with A P129BETA3P and L132BETA3L Mutated Yap PS127 Phosphopeptide, PDB code: 6g8p:

Chlorine binding site 1 out of 1 in 6g8p

Go back to Chlorine Binding Sites List in 6g8p
Chlorine binding site 1 out of 1 in the 14-3-3SIGMA in Complex with A P129BETA3P and L132BETA3L 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 P129BETA3P and L132BETA3L Mutated Yap PS127 Phosphopeptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl303

b:17.4
occ:1.00
O A:HOH693 2.9 26.2 1.0
O A:HOH635 3.1 21.3 1.0
HA A:TYR84 3.1 15.3 1.0
HD2 A:LYS87 3.2 34.0 0.4
HD3 A:LYS87 3.2 34.4 0.6
HD1 A:TYR84 3.3 16.9 1.0
HB2 A:LYS87 3.4 18.5 0.4
HD2 A:LYS87 3.4 34.4 0.6
HB2 A:LYS87 3.5 14.9 0.6
HB3 A:GLU83 3.6 17.1 1.0
CD A:LYS87 3.7 28.7 0.6
HB3 A:LYS87 3.7 14.9 0.6
HB2 A:TYR84 3.8 16.1 1.0
CA A:TYR84 3.8 12.7 1.0
HB3 A:LYS87 4.0 18.5 0.4
CD A:LYS87 4.0 28.3 0.4
CB A:LYS87 4.0 12.4 0.6
O A:GLU83 4.0 11.2 1.0
N A:TYR84 4.0 13.6 1.0
CB A:LYS87 4.0 15.4 0.4
C A:GLU83 4.1 16.8 1.0
HD3 A:LYS87 4.1 34.0 0.4
CD1 A:TYR84 4.1 14.1 1.0
CB A:TYR84 4.2 13.4 1.0
CB A:GLU83 4.4 14.2 1.0
O A:HOH494 4.4 18.8 1.0
CG A:LYS87 4.4 19.5 0.4
HB2 A:GLU83 4.5 17.1 1.0
H A:TYR84 4.5 16.3 1.0
HZ1 A:LYS87 4.5 35.3 0.6
HG3 A:LYS87 4.5 23.5 0.4
CG A:LYS87 4.5 27.9 0.6
CG A:TYR84 4.7 10.6 1.0
O A:HOH680 4.8 44.8 1.0
H A:LYS87 4.9 15.7 0.4
CA A:GLU83 4.9 14.7 1.0
HZ3 A:LYS87 4.9 35.3 0.6
CE A:LYS87 4.9 29.9 0.6
H A:LYS87 4.9 15.4 0.6
NZ A:LYS87 5.0 29.4 0.6

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 13:01:05 2020

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