Sodium in PDB 6pbc: Structural Basis For the Activation of Plc-Gamma Isozymes By Phosphorylation and Cancer-Associated Mutations

Enzymatic activity of Structural Basis For the Activation of Plc-Gamma Isozymes By Phosphorylation and Cancer-Associated Mutations

All present enzymatic activity of Structural Basis For the Activation of Plc-Gamma Isozymes By Phosphorylation and Cancer-Associated Mutations:
3.1.4.11;

Protein crystallography data

The structure of Structural Basis For the Activation of Plc-Gamma Isozymes By Phosphorylation and Cancer-Associated Mutations, PDB code: 6pbc was solved by N.Hajicek, J.Sondek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.22 / 2.46
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 70.766, 82.441, 228.318, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 24.5

Other elements in 6pbc:

The structure of Structural Basis For the Activation of Plc-Gamma Isozymes By Phosphorylation and Cancer-Associated Mutations also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Structural Basis For the Activation of Plc-Gamma Isozymes By Phosphorylation and Cancer-Associated Mutations (pdb code 6pbc). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Structural Basis For the Activation of Plc-Gamma Isozymes By Phosphorylation and Cancer-Associated Mutations, PDB code: 6pbc:

Sodium binding site 1 out of 1 in 6pbc

Go back to Sodium Binding Sites List in 6pbc
Sodium binding site 1 out of 1 in the Structural Basis For the Activation of Plc-Gamma Isozymes By Phosphorylation and Cancer-Associated Mutations


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structural Basis For the Activation of Plc-Gamma Isozymes By Phosphorylation and Cancer-Associated Mutations within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1302

b:56.6
occ:1.00
 O A:ASP96 2.4 58.3 1.0
O A:TYR93 2.7 56.1 1.0
O A:PHE99 2.7 52.7 1.0
HG2 A:ARG100 2.8 64.9 1.0
HA A:PRO97 3.0 66.0 1.0
HA A:ARG100 3.1 64.5 1.0
C A:ASP96 3.4 57.1 1.0
HG3 A:ARG100 3.5 64.9 1.0
CG A:ARG100 3.6 54.1 1.0
O A:GLN94 3.6 61.1 1.0
C A:PHE99 3.7 51.9 1.0
O A:GLU95 3.8 63.4 1.0
CA A:PRO97 3.8 55.0 1.0
C A:TYR93 3.8 53.1 1.0
CA A:ARG100 3.9 53.7 1.0
C A:GLN94 4.0 60.2 1.0
N A:PRO97 4.0 57.2 1.0
C A:GLU95 4.0 61.4 1.0
HB3 A:TYR93 4.1 58.9 1.0
HD2 A:PRO101 4.1 61.1 1.0
HA A:GLN94 4.2 69.6 1.0
CB A:ARG100 4.2 52.4 1.0
H A:PHE99 4.2 62.6 1.0
N A:ARG100 4.3 50.8 1.0
N A:ASP96 4.4 57.3 1.0
C A:PRO97 4.5 52.3 1.0
CA A:GLN94 4.5 58.0 1.0
N A:GLU95 4.5 62.6 1.0
CA A:ASP96 4.5 55.4 1.0
HB3 A:ARG100 4.5 62.9 1.0
HD3 A:PRO101 4.6 61.1 1.0
N A:GLN94 4.6 52.4 1.0
HH11 A:ARG100 4.7 69.0 1.0
CA A:GLU95 4.7 64.2 1.0
HA A:GLU95 4.7 77.1 1.0
CD A:PRO101 4.7 50.9 1.0
CD A:ARG100 4.7 51.0 1.0
CA A:TYR93 4.8 49.3 1.0
CB A:TYR93 4.8 49.1 1.0
N A:PHE99 4.8 52.2 1.0
HB3 A:ASP96 4.8 64.7 1.0
HB3 A:PRO97 4.8 63.3 1.0
HA A:TYR93 4.9 59.2 1.0
NH1 A:ARG100 4.9 57.5 1.0
H A:ASP96 4.9 68.8 1.0
O A:PRO97 4.9 51.2 1.0
NE A:ARG100 4.9 57.1 1.0
CA A:PHE99 4.9 51.8 1.0
CZ A:ARG100 5.0 57.4 1.0
CB A:PRO97 5.0 52.7 1.0
HD3 A:ARG100 5.0 61.2 1.0

Reference:

N.Hajicek, N.C.Keith, E.Siraliev-Perez, B.R.S.Temple, W.Huang, Q.Zhang, T.K.Harden, J.Sondek. Structural Basis For the Activation of Plc-Gamma Isozymes By Phosphorylation and Cancer-Associated Mutations. Elife V. 8 2019.
ISSN: ESSN 2050-084X
PubMed: 31889510
DOI: 10.7554/ELIFE.51700
Page generated: Tue Dec 15 12:44:59 2020

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