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Magnesium in PDB 7pgi: NAVAB1P (Bicelles)

Protein crystallography data

The structure of NAVAB1P (Bicelles), PDB code: 7pgi was solved by M.Lolicato, C.Arrigoni, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.99 / 3.64
Space group I 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 178.18, 191.8, 192.32, 90, 90, 90
R / Rfree (%) 28.7 / 30.4

Other elements in 7pgi:

The structure of NAVAB1P (Bicelles) also contains other interesting chemical elements:

Sodium (Na) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the NAVAB1P (Bicelles) (pdb code 7pgi). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the NAVAB1P (Bicelles), PDB code: 7pgi:

Magnesium binding site 1 out of 1 in 7pgi

Go back to Magnesium Binding Sites List in 7pgi
Magnesium binding site 1 out of 1 in the NAVAB1P (Bicelles)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of NAVAB1P (Bicelles) within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg301

b:113.3
occ:1.00
CA E:VAL271 2.6 146.7 1.0
CB E:VAL271 2.9 146.2 1.0
CG2 E:VAL271 2.9 123.5 1.0
CG1 E:VAL271 2.9 164.9 1.0
OE1 E:GLU274 3.3 174.0 1.0
O E:VAL271 3.6 176.3 1.0
C E:VAL271 3.6 166.2 1.0
CD H:LYS269 3.6 148.5 1.0
N E:VAL271 3.6 144.3 1.0
CB E:GLU274 3.8 153.5 1.0
CE H:LYS269 4.0 107.3 1.0
CD E:GLU274 4.1 167.9 1.0
O E:ILE270 4.1 158.3 1.0
NZ H:LYS269 4.2 77.8 1.0
C E:ILE270 4.2 143.4 1.0
CG E:GLU274 4.4 154.4 1.0
CG H:LYS269 4.8 122.1 1.0
N E:ALA272 4.8 172.3 1.0
CA E:GLU274 4.9 168.9 1.0

Reference:

C.Arrigoni, M.Lolicato, D.Shaya, A.Rohaim, F.Findeisen, L.K.Fong, C.M.Colleran, P.Dominik, S.S.Kim, J.P.Schuermann, W.F.Degrado, M.Grabe, A.A.Kossiakoff, D.L.Minor Jr.. Quaternary Structure Independent Folding of Voltage-Gated Ion Channel Pore Domain Subunits. Nat.Struct.Mol.Biol. V. 29 537 2022.
ISSN: ESSN 1545-9985
PubMed: 35655098
DOI: 10.1038/S41594-022-00775-X
Page generated: Thu Oct 3 04:09:51 2024

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