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Sodium in PDB 5l0i: Human Metavinculin Mvt R975W Cardiomyopathy-Associated Mutant (Residues 959-1134)

Protein crystallography data

The structure of Human Metavinculin Mvt R975W Cardiomyopathy-Associated Mutant (Residues 959-1134), PDB code: 5l0i was solved by K.Chinthalapudi, T.Izard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.78 / 2.45
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.074, 41.519, 44.148, 90.00, 96.14, 90.00
R / Rfree (%) 19.5 / 23.8

Sodium Binding Sites:

The binding sites of Sodium atom in the Human Metavinculin Mvt R975W Cardiomyopathy-Associated Mutant (Residues 959-1134) (pdb code 5l0i). 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 Human Metavinculin Mvt R975W Cardiomyopathy-Associated Mutant (Residues 959-1134), PDB code: 5l0i:

Sodium binding site 1 out of 1 in 5l0i

Go back to Sodium Binding Sites List in 5l0i
Sodium binding site 1 out of 1 in the Human Metavinculin Mvt R975W Cardiomyopathy-Associated Mutant (Residues 959-1134)


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Human Metavinculin Mvt R975W Cardiomyopathy-Associated Mutant (Residues 959-1134) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na2501

b:34.1
occ:1.00
O A:HOH2619 3.0 33.6 1.0
N A:THR1130 3.4 20.2 1.0
CA A:LYS1129 3.9 18.2 1.0
CB A:LYS1129 3.9 19.1 1.0
OG1 A:THR1130 4.0 24.2 1.0
CB A:THR1130 4.1 22.8 1.0
C A:LYS1129 4.2 22.7 1.0
CE A:LYS1129 4.2 51.9 1.0
CG A:LYS1129 4.4 23.2 1.0
CA A:THR1130 4.4 19.7 1.0
CD A:LYS1129 4.9 38.4 1.0
O A:THR1130 4.9 22.6 1.0

Reference:

K.Chinthalapudi, E.S.Rangarajan, D.T.Brown, T.Izard. Differential Lipid Binding of Vinculin Isoforms Promotes Quasi-Equivalent Dimerization. Proc.Natl.Acad.Sci.Usa V. 113 9539 2016.
ISSN: ESSN 1091-6490
PubMed: 27503891
DOI: 10.1073/PNAS.1600702113
Page generated: Tue Dec 15 11:12:07 2020

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