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Chlorine in PDB 8rrm: Tripartite Complex Between 14-3-3 Sigma, Fusicoccin-A, and A Phosphopeptide Optimized For A Fusicoccin-Mediated Stabilization of the Complex

Protein crystallography data

The structure of Tripartite Complex Between 14-3-3 Sigma, Fusicoccin-A, and A Phosphopeptide Optimized For A Fusicoccin-Mediated Stabilization of the Complex, PDB code: 8rrm was solved by A.Cousido-Siah, A.G.Mcewen, E.Monsellier, G.Trave, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.44 / 2.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 138.33, 55.91, 82.75, 90, 101.71, 90
R / Rfree (%) 18.3 / 21.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Tripartite Complex Between 14-3-3 Sigma, Fusicoccin-A, and A Phosphopeptide Optimized For A Fusicoccin-Mediated Stabilization of the Complex (pdb code 8rrm). 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 Tripartite Complex Between 14-3-3 Sigma, Fusicoccin-A, and A Phosphopeptide Optimized For A Fusicoccin-Mediated Stabilization of the Complex, PDB code: 8rrm:

Chlorine binding site 1 out of 1 in 8rrm

Go back to Chlorine Binding Sites List in 8rrm
Chlorine binding site 1 out of 1 in the Tripartite Complex Between 14-3-3 Sigma, Fusicoccin-A, and A Phosphopeptide Optimized For A Fusicoccin-Mediated Stabilization of the Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Tripartite Complex Between 14-3-3 Sigma, Fusicoccin-A, and A Phosphopeptide Optimized For A Fusicoccin-Mediated Stabilization of the Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl302

b:56.4
occ:1.00
HZ3 B:LYS9 2.2 61.5 1.0
O A:HOH494 2.8 64.2 1.0
HA A:TYR84 2.9 56.9 1.0
NZ B:LYS9 3.1 51.3 1.0
HD1 A:TYR84 3.1 54.2 1.0
HZ B:PHE25 3.2 58.4 1.0
HD3 B:LYS9 3.2 54.6 1.0
HZ2 B:LYS9 3.5 61.5 1.0
HD2 A:LYS87 3.5 86.3 1.0
HZ1 B:LYS9 3.5 61.5 1.0
HB2 A:TYR84 3.7 55.4 1.0
CA A:TYR84 3.7 47.4 1.0
HB2 A:LYS87 3.7 61.7 1.0
HB3 A:GLU83 3.7 66.0 1.0
HE1 B:PHE25 3.9 60.4 1.0
CE B:LYS9 3.9 48.9 1.0
HE2 B:LYS9 3.9 58.7 1.0
N A:TYR84 3.9 49.2 1.0
O A:GLU83 3.9 55.5 1.0
HB3 A:LYS87 3.9 61.7 1.0
CD1 A:TYR84 4.0 45.2 1.0
CD B:LYS9 4.0 45.5 1.0
CZ B:PHE25 4.0 48.6 1.0
HD3 A:LYS87 4.0 86.3 1.0
C A:GLU83 4.0 54.2 1.0
CB A:TYR84 4.1 46.1 1.0
CD A:LYS87 4.1 71.9 1.0
CB A:LYS87 4.3 51.4 1.0
CE1 B:PHE25 4.3 50.3 1.0
HD2 B:LYS9 4.4 54.6 1.0
H A:TYR84 4.4 59.0 1.0
HB2 A:GLU83 4.5 66.0 1.0
CB A:GLU83 4.5 55.0 1.0
CG A:TYR84 4.5 46.8 1.0
O A:HOH422 4.5 58.6 1.0
O B:HOH445 4.6 54.5 1.0
HE3 B:LYS9 4.8 58.7 1.0
CG A:LYS87 4.8 54.2 1.0
CA A:GLU83 4.9 56.6 1.0
C A:TYR84 4.9 50.7 1.0
CE1 A:TYR84 5.0 47.8 1.0
HB3 A:TYR84 5.0 55.4 1.0

Reference:

F.Delalande, G.Gogl, A.Cousido-Siah, A.G.Mcewen, A.Rohrbacher, C.Kostmann, Y.Nomine, P.Eberling, C.Carapito, G.Trave, E.Monsellier. Holdup Multiplex Assay For High-Throughput Measurement of Protein-Ligand Affinity Constants Using A Mass-Spectrometry Readout To Be Published.
Page generated: Tue Feb 25 09:08:34 2025

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