Magnesium in PDB 8gj8: RAD51C C-Terminal Domain

Protein crystallography data

The structure of RAD51C C-Terminal Domain, PDB code: 8gj8 was solved by A.S.Arvai, J.A.Tainer, G.Williams, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.36 / 2.30
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 96.032, 96.032, 55.683, 90, 90, 120
R / Rfree (%) 18.8 / 23.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the RAD51C C-Terminal Domain (pdb code 8gj8). 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 RAD51C C-Terminal Domain, PDB code: 8gj8:

Magnesium binding site 1 out of 1 in 8gj8

Go back to Magnesium Binding Sites List in 8gj8
Magnesium binding site 1 out of 1 in the RAD51C C-Terminal Domain


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of RAD51C C-Terminal Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:40.1
occ:1.00
O2B A:ADP402 2.0 41.4 1.0
O A:HOH506 2.0 38.1 1.0
O A:HOH511 2.1 39.4 1.0
O A:HOH509 2.2 41.2 1.0
O A:HOH514 2.2 36.0 1.0
OG1 A:THR124 2.2 35.4 1.0
PB A:ADP402 3.1 41.3 1.0
CB A:THR124 3.3 38.4 1.0
O1B A:ADP402 3.3 41.6 1.0
O1A A:ADP402 4.0 46.4 1.0
O A:HOH513 4.1 49.0 1.0
OE1 A:GLU153 4.1 65.3 1.0
OD1 A:ASP234 4.1 44.0 1.0
N A:THR124 4.1 35.8 1.0
O3A A:ADP402 4.2 38.5 1.0
O3B A:ADP402 4.2 39.2 1.0
CA A:THR124 4.3 37.5 1.0
CG2 A:THR124 4.4 39.2 1.0
OD2 A:ASP234 4.4 46.0 1.0
PA A:ADP402 4.4 43.9 1.0
O A:HOH526 4.5 50.4 1.0
O A:HOH538 4.6 53.5 1.0
O2A A:ADP402 4.6 50.8 1.0
CG A:ASP234 4.7 42.2 1.0
CB A:LYS123 4.8 33.0 1.0
CD A:GLU153 5.0 57.4 1.0

Reference:

M.A.Longo, S.Roy, Y.Chen, K.H.Tomaszowski, A.S.Arvai, J.T.Pepper, R.A.Boisvert, S.Kunnimalaiyaan, C.Keshvani, D.Schild, A.Bacolla, G.J.Williams, J.A.Tainer, K.Schlacher. RAD51C-XRCC3 Structure and Cancer Patient Mutations Define Dna Replication Roles. Nat Commun V. 14 4445 2023.
ISSN: ESSN 2041-1723
PubMed: 37488098
DOI: 10.1038/S41467-023-40096-1
Page generated: Fri Oct 4 03:51:18 2024

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