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Calcium in PDB 5o2z: Domain Swap Dimer of the G167R Variant of Gelsolin Second Domain

Protein crystallography data

The structure of Domain Swap Dimer of the G167R Variant of Gelsolin Second Domain, PDB code: 5o2z was solved by F.Boni, M.Milani, E.Mastrangelo, M.De Rosa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.39 / 1.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 106.290, 44.420, 58.010, 90.00, 110.13, 90.00
R / Rfree (%) 19.9 / 24.2

Other elements in 5o2z:

The structure of Domain Swap Dimer of the G167R Variant of Gelsolin Second Domain also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Domain Swap Dimer of the G167R Variant of Gelsolin Second Domain (pdb code 5o2z). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Domain Swap Dimer of the G167R Variant of Gelsolin Second Domain, PDB code: 5o2z:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 5o2z

Go back to Calcium Binding Sites List in 5o2z
Calcium binding site 1 out of 2 in the Domain Swap Dimer of the G167R Variant of Gelsolin Second Domain


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Domain Swap Dimer of the G167R Variant of Gelsolin Second Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca301

b:22.4
occ:1.00
OG1 B:FLC302 2.3 27.3 1.0
O B:GLY186 2.4 23.4 1.0
OD1 B:ASP187 2.4 22.2 1.0
OE2 B:GLU209 2.4 25.9 1.0
OB1 B:FLC302 2.4 17.6 1.0
OHB B:FLC302 2.5 27.1 1.0
O B:HOH413 2.6 26.9 1.0
OE1 B:GLU209 2.6 24.0 1.0
CD B:GLU209 2.9 22.1 1.0
CBC B:FLC302 3.1 25.4 1.0
CB B:FLC302 3.2 26.9 1.0
CGC B:FLC302 3.3 24.7 1.0
C B:GLY186 3.4 24.6 1.0
CG B:ASP187 3.6 19.8 1.0
CG B:FLC302 3.7 26.0 1.0
ND2 B:ASN206 3.9 27.6 1.0
CA B:ASP187 4.1 16.8 1.0
N B:ASP187 4.1 18.2 1.0
OB2 B:FLC302 4.2 27.1 1.0
O B:HOH430 4.3 28.4 1.0
CG B:GLU209 4.4 23.6 1.0
CA B:GLY186 4.4 24.4 1.0
OG2 B:FLC302 4.4 30.7 1.0
CB B:ASP187 4.4 15.9 1.0
NZ A:LYS166 4.4 24.4 1.0
OD2 B:ASP187 4.5 24.0 1.0
CA B:FLC302 4.7 27.8 1.0
CA B:SER205 4.7 27.1 1.0
CG A:LYS166 4.7 20.2 1.0
O B:ASN204 4.7 23.5 1.0
N A:ARG167 4.8 20.6 1.0
O B:HOH461 4.8 51.5 1.0
N B:ASN206 4.9 19.9 1.0
CG B:ASN206 4.9 24.1 1.0
OA1 B:FLC302 4.9 31.2 1.0
O A:ARG167 5.0 21.6 1.0

Calcium binding site 2 out of 2 in 5o2z

Go back to Calcium Binding Sites List in 5o2z
Calcium binding site 2 out of 2 in the Domain Swap Dimer of the G167R Variant of Gelsolin Second Domain


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Domain Swap Dimer of the G167R Variant of Gelsolin Second Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca301

b:19.2
occ:1.00
OE1 A:GLU209 2.3 20.3 1.0
OG2 A:FLC302 2.4 24.4 1.0
O A:GLY186 2.4 23.1 1.0
OD2 A:ASP187 2.4 19.0 1.0
OB2 A:FLC302 2.5 25.8 1.0
OHB A:FLC302 2.5 25.6 1.0
OE2 A:GLU209 2.7 20.9 1.0
O B:HOH422 2.7 18.8 1.0
CD A:GLU209 2.8 21.4 1.0
CBC A:FLC302 3.1 35.9 1.0
CB A:FLC302 3.2 33.5 1.0
CGC A:FLC302 3.3 30.9 1.0
C A:GLY186 3.4 23.2 1.0
CG A:ASP187 3.6 22.8 1.0
CG A:FLC302 3.7 31.5 1.0
ND2 A:ASN206 3.9 25.6 1.0
CA A:ASP187 4.1 19.4 1.0
N A:ASP187 4.2 21.4 1.0
OB1 A:FLC302 4.2 32.4 1.0
CG A:GLU209 4.3 22.6 1.0
NZ B:LYS166 4.4 22.6 1.0
O A:HOH413 4.4 25.2 1.0
CB A:ASP187 4.4 17.8 1.0
CA A:GLY186 4.4 18.5 1.0
OG1 A:FLC302 4.4 33.3 1.0
OD1 A:ASP187 4.5 27.3 1.0
CA A:SER205 4.7 27.9 1.0
CA A:FLC302 4.7 32.1 1.0
O A:ASN204 4.7 24.3 1.0
N B:ARG167 4.7 19.4 1.0
CG B:LYS166 4.8 23.3 1.0
N A:ASN206 4.8 20.6 1.0
CG A:ASN206 4.9 28.9 1.0
O B:ARG167 4.9 23.5 1.0
OA1 A:FLC302 4.9 32.9 1.0
NH2 A:ARG167 5.0 25.2 1.0

Reference:

F.Boni, M.Milani, A.Barbiroli, L.Diomede, E.Mastrangelo, M.De Rosa. Gelsolin Pathogenic GLY167ARG Mutation Promotes Domain-Swap Dimerization of the Protein. Hum. Mol. Genet. V. 27 53 2018.
ISSN: ESSN 1460-2083
PubMed: 29069428
DOI: 10.1093/HMG/DDX383
Page generated: Mon Jul 15 09:41:32 2024

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