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Sodium in PDB 3e7b: Crystal Structure of Protein Phosphatase-1 Bound to the Natural Toxin Inhibitor Tautomycin

Enzymatic activity of Crystal Structure of Protein Phosphatase-1 Bound to the Natural Toxin Inhibitor Tautomycin

All present enzymatic activity of Crystal Structure of Protein Phosphatase-1 Bound to the Natural Toxin Inhibitor Tautomycin:
3.1.3.16;

Protein crystallography data

The structure of Crystal Structure of Protein Phosphatase-1 Bound to the Natural Toxin Inhibitor Tautomycin, PDB code: 3e7b was solved by M.S.Kelker, R.Page, W.Peti, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.63 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 65.760, 78.519, 130.764, 90.00, 90.00, 90.00
R / Rfree (%) 15.3 / 17.5

Other elements in 3e7b:

The structure of Crystal Structure of Protein Phosphatase-1 Bound to the Natural Toxin Inhibitor Tautomycin also contains other interesting chemical elements:

Manganese (Mn) 4 atoms
Chlorine (Cl) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Protein Phosphatase-1 Bound to the Natural Toxin Inhibitor Tautomycin (pdb code 3e7b). 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 Crystal Structure of Protein Phosphatase-1 Bound to the Natural Toxin Inhibitor Tautomycin, PDB code: 3e7b:

Sodium binding site 1 out of 1 in 3e7b

Go back to Sodium Binding Sites List in 3e7b
Sodium binding site 1 out of 1 in the Crystal Structure of Protein Phosphatase-1 Bound to the Natural Toxin Inhibitor Tautomycin


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Protein Phosphatase-1 Bound to the Natural Toxin Inhibitor Tautomycin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na502

b:23.4
occ:1.00
 O A:SER85 2.8 19.9 1.0
O A:ASN117 2.9 16.8 1.0
CB A:PRO82 3.5 18.8 1.0
CD2 A:PHE118 3.7 17.3 1.0
CA A:PRO83 3.7 19.9 1.0
C A:ASN117 3.7 17.4 1.0
CA A:PRO82 3.8 17.8 1.0
CA A:ASN86 3.8 17.8 1.0
C A:SER85 3.8 19.5 1.0
CD2 A:TYR87 3.9 18.2 1.0
CB A:PHE118 4.0 18.7 1.0
N A:TYR87 4.0 16.1 1.0
CG A:PRO82 4.0 19.5 1.0
CB A:ASN117 4.2 18.3 1.0
C A:ASN86 4.2 19.8 1.0
N A:ASN86 4.2 18.4 1.0
CA A:PHE118 4.2 19.0 1.0
CG A:PHE118 4.3 17.1 1.0
N A:PHE118 4.4 17.4 1.0
C A:PRO83 4.4 19.8 1.0
CB A:PRO83 4.4 20.8 1.0
N A:PRO83 4.5 17.1 1.0
C A:PRO82 4.6 19.7 1.0
CA A:ASN117 4.6 17.9 1.0
OD1 A:ASN86 4.6 20.8 1.0
CE2 A:TYR87 4.7 17.9 1.0
CB A:TYR87 4.7 16.6 1.0
CB A:TYR114 4.7 17.9 1.0
O A:PRO83 4.7 18.4 1.0
CE2 A:PHE118 4.7 20.1 1.0
CG A:TYR87 4.8 17.4 1.0
N A:PRO82 4.9 17.6 1.0
CD2 A:TYR114 5.0 16.9 1.0
CA A:TYR87 5.0 16.5 1.0
CB A:ASN86 5.0 19.1 1.0

Reference:

M.S.Kelker, R.Page, W.Peti. Crystal Structures of Protein Phosphatase-1 Bound to Nodularin-R and Tautomycin: A Novel Scaffold For Structure-Based Drug Design of Serine/Threonine Phosphatase Inhibitors J.Mol.Biol. V. 385 11 2009.
ISSN: ISSN 0022-2836
PubMed: 18992256
DOI: 10.1016/J.JMB.2008.10.053
Page generated: Mon Oct 7 08:48:26 2024

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