Atomistry » Sodium » PDB 3iwf-3k93 » 3k6n
Atomistry »
  Sodium »
    PDB 3iwf-3k93 »
      3k6n »

Sodium in PDB 3k6n: Crystal Structure of the S225E Mutant KIR3.1 Cytoplasmic Pore Domain

Protein crystallography data

The structure of Crystal Structure of the S225E Mutant KIR3.1 Cytoplasmic Pore Domain, PDB code: 3k6n was solved by Y.Xu, H.G.Shin, S.Szep, Z.Lu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 2.00
Space group P 4 21 2
Cell size a, b, c (Å), α, β, γ (°) 77.455, 77.455, 86.723, 90.00, 90.00, 90.00
R / Rfree (%) 25.4 / 26.6

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of the S225E Mutant KIR3.1 Cytoplasmic Pore Domain (pdb code 3k6n). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 5 binding sites of Sodium where determined in the Crystal Structure of the S225E Mutant KIR3.1 Cytoplasmic Pore Domain, PDB code: 3k6n:
Jump to Sodium binding site number: 1; 2; 3; 4; 5;

Sodium binding site 1 out of 5 in 3k6n

Go back to Sodium Binding Sites List in 3k6n
Sodium binding site 1 out of 5 in the Crystal Structure of the S225E Mutant KIR3.1 Cytoplasmic Pore Domain


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 the S225E Mutant KIR3.1 Cytoplasmic Pore Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na7

b:90.0
occ:0.25
O A:HOH529 3.6 78.6 1.0

Sodium binding site 2 out of 5 in 3k6n

Go back to Sodium Binding Sites List in 3k6n
Sodium binding site 2 out of 5 in the Crystal Structure of the S225E Mutant KIR3.1 Cytoplasmic Pore Domain


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Crystal Structure of the S225E Mutant KIR3.1 Cytoplasmic Pore Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na8

b:78.9
occ:0.25
O A:HOH510 2.7 69.2 1.0
OE2 A:GLU225 4.1 74.8 1.0
OE1 A:GLU225 4.1 75.0 1.0
CD A:GLU225 4.5 74.1 1.0
O A:HOH526 4.8 80.1 1.0

Sodium binding site 3 out of 5 in 3k6n

Go back to Sodium Binding Sites List in 3k6n
Sodium binding site 3 out of 5 in the Crystal Structure of the S225E Mutant KIR3.1 Cytoplasmic Pore Domain


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 3 of Crystal Structure of the S225E Mutant KIR3.1 Cytoplasmic Pore Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na9

b:69.0
occ:0.25
O A:HOH511 3.4 73.7 1.0
O A:HOH512 3.6 76.4 1.0

Sodium binding site 4 out of 5 in 3k6n

Go back to Sodium Binding Sites List in 3k6n
Sodium binding site 4 out of 5 in the Crystal Structure of the S225E Mutant KIR3.1 Cytoplasmic Pore Domain


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 4 of Crystal Structure of the S225E Mutant KIR3.1 Cytoplasmic Pore Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na10

b:81.9
occ:0.25
CZ A:PHE255 4.8 50.4 1.0
NA A:NA11 4.9 81.4 0.2

Sodium binding site 5 out of 5 in 3k6n

Go back to Sodium Binding Sites List in 3k6n
Sodium binding site 5 out of 5 in the Crystal Structure of the S225E Mutant KIR3.1 Cytoplasmic Pore Domain


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 5 of Crystal Structure of the S225E Mutant KIR3.1 Cytoplasmic Pore Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na11

b:81.4
occ:0.25
O A:HOH513 3.4 78.9 1.0
O A:HOH514 3.9 69.4 1.0
NA A:NA10 4.9 81.9 0.2

Reference:

Y.Xu, H.G.Shin, S.Szep, Z.Lu. Physical Determinants of Strong Voltage Sensitivity of K(+) Channel Block. Nat.Struct.Mol.Biol. V. 16 1252 2009.
ISSN: ISSN 1545-9993
PubMed: 19915587
DOI: 10.1038/NSMB.1717
Page generated: Mon Oct 7 11:11:03 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy