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Sodium in PDB 1bun: Structure of BETA2-Bungarotoxin: Potassium Channel Binding By Kunitz Modules and Targeted Phospholipase Action

Enzymatic activity of Structure of BETA2-Bungarotoxin: Potassium Channel Binding By Kunitz Modules and Targeted Phospholipase Action

All present enzymatic activity of Structure of BETA2-Bungarotoxin: Potassium Channel Binding By Kunitz Modules and Targeted Phospholipase Action:
3.1.1.4;

Protein crystallography data

The structure of Structure of BETA2-Bungarotoxin: Potassium Channel Binding By Kunitz Modules and Targeted Phospholipase Action, PDB code: 1bun was solved by P.D.Kwong, N.Q.Mcdonald, P.B.Sigler, W.A.Hendrickson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 5.00 / 2.45
Space group P 43 2 2
Cell size a, b, c (Å), α, β, γ (°) 52.600, 52.600, 177.500, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 28.1

Sodium Binding Sites:

The binding sites of Sodium atom in the Structure of BETA2-Bungarotoxin: Potassium Channel Binding By Kunitz Modules and Targeted Phospholipase Action (pdb code 1bun). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Structure of BETA2-Bungarotoxin: Potassium Channel Binding By Kunitz Modules and Targeted Phospholipase Action, PDB code: 1bun:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 1bun

Go back to Sodium Binding Sites List in 1bun
Sodium binding site 1 out of 2 in the Structure of BETA2-Bungarotoxin: Potassium Channel Binding By Kunitz Modules and Targeted Phospholipase Action


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of BETA2-Bungarotoxin: Potassium Channel Binding By Kunitz Modules and Targeted Phospholipase Action within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na121

b:48.7
occ:1.00
O A:GLY32 2.3 31.3 1.0
O A:GLY30 2.3 36.0 1.0
OD2 A:ASP49 2.5 34.2 1.0
O A:TYR28 2.5 21.1 1.0
OD1 A:ASP49 3.1 35.3 1.0
CG A:ASP49 3.2 32.8 1.0
C A:GLY32 3.3 32.7 1.0
N A:GLY32 3.5 35.2 1.0
C A:GLY30 3.5 36.2 1.0
C A:TYR28 3.7 20.3 1.0
CA A:GLY32 3.9 33.9 1.0
O A:HOH131 3.9 21.5 1.0
C A:ALA31 4.0 35.8 1.0
N A:GLY30 4.0 32.7 1.0
N A:ALA31 4.3 36.5 1.0
CA A:ALA31 4.3 36.0 1.0
CA A:TYR28 4.3 18.0 1.0
CA A:GLY30 4.4 34.6 1.0
N A:GLY33 4.5 30.7 1.0
CB A:TYR28 4.6 15.8 1.0
O A:ALA31 4.7 35.9 1.0
CB A:ASP49 4.7 29.5 1.0
C A:CYS29 4.7 29.9 1.0
N A:CYS29 4.8 24.1 1.0
CD2 A:TYR28 4.8 13.9 1.0
CA A:CYS29 4.9 26.2 1.0
CA A:GLY33 4.9 28.2 1.0

Sodium binding site 2 out of 2 in 1bun

Go back to Sodium Binding Sites List in 1bun
Sodium binding site 2 out of 2 in the Structure of BETA2-Bungarotoxin: Potassium Channel Binding By Kunitz Modules and Targeted Phospholipase Action


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Structure of BETA2-Bungarotoxin: Potassium Channel Binding By Kunitz Modules and Targeted Phospholipase Action within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na122

b:16.8
occ:1.00
O A:GLU105 2.6 31.6 1.0
OD2 A:ASP39 2.8 21.0 1.0
CG A:ASP39 3.0 21.9 1.0
N A:LEU41 3.2 15.3 1.0
OD1 A:ASP39 3.4 23.6 1.0
N A:ALA40 3.5 17.6 1.0
CB A:ASP39 3.6 20.0 1.0
C A:GLU105 3.7 31.0 1.0
CB A:LEU41 3.7 9.3 1.0
OH A:TYR25 3.7 17.1 1.0
CB A:ALA40 3.8 15.1 1.0
CA A:ALA40 3.9 15.6 1.0
CD1 A:ILE107 3.9 17.2 1.0
C A:ALA40 4.0 15.9 1.0
CA A:LEU41 4.0 14.2 1.0
CG1 A:ILE107 4.1 20.9 1.0
CB A:GLU105 4.2 39.2 1.0
C A:ASP39 4.2 18.6 1.0
O A:HOH152 4.3 42.9 1.0
CA A:GLU105 4.3 33.5 1.0
N A:GLU105 4.3 32.5 1.0
N A:ILE107 4.4 26.3 1.0
O A:HOH150 4.5 38.3 1.0
CA A:ASP39 4.5 19.0 1.0
CB A:ILE107 4.7 23.4 1.0
N A:TYR106 4.7 28.3 1.0
CZ A:TYR25 4.8 18.3 1.0
CA A:TYR106 4.9 26.7 1.0
CE1 A:TYR25 5.0 18.6 1.0
CB A:SER104 5.0 33.4 1.0

Reference:

P.D.Kwong, N.Q.Mcdonald, P.B.Sigler, W.A.Hendrickson. Structure of Beta 2-Bungarotoxin: Potassium Channel Binding By Kunitz Modules and Targeted Phospholipase Action. Structure V. 3 1109 1995.
ISSN: ISSN 0969-2126
PubMed: 8590005
DOI: 10.1016/S0969-2126(01)00246-5
Page generated: Sun Aug 17 04:47:31 2025

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