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Sodium in PDB 4l76: CA2+-Bound E212Q Mutant Mthk Rck Domain

Protein crystallography data

The structure of CA2+-Bound E212Q Mutant Mthk Rck Domain, PDB code: 4l76 was solved by F.J.Smith, B.S.Rothberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.56 / 2.99
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 118.884, 118.884, 356.052, 90.00, 90.00, 120.00
R / Rfree (%) 21.7 / 26.3

Other elements in 4l76:

The structure of CA2+-Bound E212Q Mutant Mthk Rck Domain also contains other interesting chemical elements:

Calcium (Ca) 13 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the CA2+-Bound E212Q Mutant Mthk Rck Domain (pdb code 4l76). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the CA2+-Bound E212Q Mutant Mthk Rck Domain, PDB code: 4l76:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 4l76

Go back to Sodium Binding Sites List in 4l76
Sodium binding site 1 out of 2 in the CA2+-Bound E212Q Mutant Mthk Rck Domain


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of CA2+-Bound E212Q Mutant Mthk Rck Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na403

b:71.8
occ:1.00
OD2 B:ASP202 2.5 0.5 1.0
N B:GLY177 2.7 0.4 1.0
CA B:GLY177 3.3 0.8 1.0
CG B:ASP202 3.6 0.8 1.0
C B:ARG176 3.7 0.2 1.0
CA B:ARG176 4.0 97.6 1.0
OD1 B:ASP202 4.2 0.9 1.0
C B:GLY177 4.2 0.6 1.0
N B:ALA178 4.3 92.0 1.0
NH1 B:ARG116 4.3 0.3 1.0
O B:ALA178 4.4 91.3 1.0
O B:VAL175 4.5 80.3 1.0
CB B:ASP202 4.7 0.1 1.0
CB B:ARG176 4.8 0.7 1.0
O B:ARG176 4.9 0.1 1.0
CB B:VAL205 4.9 78.8 1.0

Sodium binding site 2 out of 2 in 4l76

Go back to Sodium Binding Sites List in 4l76
Sodium binding site 2 out of 2 in the CA2+-Bound E212Q Mutant Mthk Rck Domain


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of CA2+-Bound E212Q Mutant Mthk Rck Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Na403

b:88.3
occ:1.00
O D:GLY156 2.6 0.8 1.0
O D:SER137 2.7 0.9 1.0
C D:GLY156 3.6 0.9 1.0
N D:VAL139 3.7 0.8 1.0
CA D:GLU138 3.7 0.1 1.0
C D:SER137 3.8 0.6 1.0
CA D:ALA157 4.0 91.0 1.0
N D:ALA157 4.2 0.2 1.0
N D:GLU138 4.2 0.3 1.0
C D:GLU138 4.2 0.9 1.0
CA D:GLY156 4.6 0.9 1.0
O D:VAL139 4.7 87.6 1.0
C D:ALA157 4.7 91.4 1.0
CA D:VAL139 4.8 0.7 1.0
CB D:GLU138 4.8 99.5 1.0
CB D:VAL139 4.9 85.2 1.0
N D:ASN158 4.9 98.5 1.0

Reference:

F.J.Smith, V.P.Pau, G.Cingolani, B.S.Rothberg. Structural Basis of Allosteric Interactions Among Ca(2+)-Binding Sites in A K(+) Channel Rck Domain. Nat Commun V. 4 2621 2013.
ISSN: ESSN 2041-1723
PubMed: 24126388
DOI: 10.1038/NCOMMS3621
Page generated: Mon Oct 7 16:42:03 2024

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