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Sodium in PDB 4c0k: Crystal Structure of Drosophila Miro Ef Hand and Cgtpase Domains Bound to One Calcium Ion (Ca-Miros)

Protein crystallography data

The structure of Crystal Structure of Drosophila Miro Ef Hand and Cgtpase Domains Bound to One Calcium Ion (Ca-Miros), PDB code: 4c0k was solved by J.L.Klosowiak, P.J.Focia, Z.Wawrzak, S.Chakravarthy, E.C.Landahl, D.M.Freymann, S.E.Rice, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.075 / 2.80
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 82.240, 82.240, 156.441, 90.00, 90.00, 120.00
R / Rfree (%) 20.72 / 24.22

Other elements in 4c0k:

The structure of Crystal Structure of Drosophila Miro Ef Hand and Cgtpase Domains Bound to One Calcium Ion (Ca-Miros) also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Drosophila Miro Ef Hand and Cgtpase Domains Bound to One Calcium Ion (Ca-Miros) (pdb code 4c0k). 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 Drosophila Miro Ef Hand and Cgtpase Domains Bound to One Calcium Ion (Ca-Miros), PDB code: 4c0k:

Sodium binding site 1 out of 1 in 4c0k

Go back to Sodium Binding Sites List in 4c0k
Sodium binding site 1 out of 1 in the Crystal Structure of Drosophila Miro Ef Hand and Cgtpase Domains Bound to One Calcium Ion (Ca-Miros)


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 Drosophila Miro Ef Hand and Cgtpase Domains Bound to One Calcium Ion (Ca-Miros) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1614

b:52.0
occ:1.00
OD1 A:ASP227 2.4 42.2 1.0
OD1 A:ASP223 2.5 45.5 1.0
O A:LEU229 2.7 38.7 1.0
OE2 A:GLU234 3.0 42.2 1.0
CB A:ASP225 3.1 40.9 1.0
N A:ASP225 3.2 42.0 1.0
OD2 A:ASP225 3.3 48.8 1.0
CG A:ASP227 3.4 42.5 1.0
ND2 A:ASN231 3.5 48.0 1.0
CG A:ASP225 3.6 47.8 1.0
CA A:ASP225 3.7 39.1 1.0
CG A:ASP223 3.7 41.5 1.0
N A:ILE224 3.8 36.0 1.0
C A:LEU229 3.8 42.8 1.0
OD2 A:ASP227 3.8 42.9 1.0
CA A:ASP223 4.0 35.2 1.0
C A:ASP223 4.0 37.9 1.0
CD A:GLU234 4.1 41.9 1.0
N A:GLY226 4.2 36.7 1.0
C A:ASP225 4.2 41.2 1.0
C A:ILE224 4.3 39.2 1.0
N A:ASP227 4.4 42.6 1.0
CB A:ASP223 4.4 37.9 1.0
N A:LEU229 4.5 44.9 1.0
CG1 A:ILE224 4.6 32.1 1.0
OD2 A:ASP223 4.6 43.7 1.0
CA A:ILE224 4.6 35.4 1.0
OD1 A:ASP225 4.6 50.7 1.0
CA A:LEU229 4.6 42.5 1.0
N A:ASN231 4.6 39.2 1.0
O A:ASP223 4.7 38.4 1.0
CG A:ASN231 4.7 47.1 1.0
CB A:ASP227 4.7 47.2 1.0
N A:LEU230 4.7 41.4 1.0
CA A:LEU230 4.8 37.2 1.0
OE1 A:GLU234 4.8 43.7 1.0
CB A:LEU229 4.9 43.7 1.0
CG A:GLU234 4.9 35.8 1.0
O A:CYS222 5.0 34.3 1.0

Reference:

J.L.Klosowiak, P.J.Focia, S.Chakravarthy, E.C.Landahl, D.M.Freymann, S.E.Rice. Structural Coupling of the Ef Hand and C-Terminal Gtpase Domains in the Mitochondrial Protein Miro. Embo Rep. V. 14 968 2013.
ISSN: ISSN 1469-221X
PubMed: 24071720
DOI: 10.1038/EMBOR.2013.151
Page generated: Sun Aug 17 18:41:37 2025

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