Magnesium in PDB 7p0j: Crystal Structure of S.Pombe MDB1 Brct Domains

Protein crystallography data

The structure of Crystal Structure of S.Pombe MDB1 Brct Domains, PDB code: 7p0j was solved by M.Day, A.W.Oliver, L.H.Pearl, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.82 / 1.48
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 114.18, 44.12, 49.86, 90, 92.37, 90
R / Rfree (%) 17 / 19.7

Other elements in 7p0j:

The structure of Crystal Structure of S.Pombe MDB1 Brct Domains also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of S.Pombe MDB1 Brct Domains (pdb code 7p0j). 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 Crystal Structure of S.Pombe MDB1 Brct Domains, PDB code: 7p0j:

Magnesium binding site 1 out of 1 in 7p0j

Go back to Magnesium Binding Sites List in 7p0j
Magnesium binding site 1 out of 1 in the Crystal Structure of S.Pombe MDB1 Brct Domains


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of S.Pombe MDB1 Brct Domains within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg604

b:40.9
occ:0.50
O A:HOH930 2.0 26.0 0.6
O A:HOH722 2.1 25.3 0.9
O2 A:CIT601 2.8 26.8 1.0
C1 A:CIT601 3.5 23.8 1.0
HO7 A:CIT601 3.6 17.1 1.0
HZ2 A:LYS434 3.8 22.4 1.0
O1 A:CIT601 3.8 22.8 1.0
O A:HOH835 3.9 25.3 0.7
HZ1 A:LYS434 4.2 22.4 1.0
O7 A:CIT601 4.4 14.3 1.0
NZ A:LYS434 4.4 18.7 1.0
O A:HOH742 4.5 17.9 1.0
O5 A:CIT601 4.5 14.9 1.0
C2 A:CIT601 4.6 16.3 1.0
HZ3 A:LYS434 4.8 22.4 1.0
H21 A:CIT601 4.9 19.6 1.0
C3 A:CIT601 4.9 14.7 1.0
C6 A:CIT601 4.9 15.4 1.0

Reference:

M.Day, A.W.Oliver, L.H.Pearl. The Role of TOPBP1 in Phosphorylation-Dependent Assembly of Dna Damage Response Systems To Be Published.
Page generated: Thu Apr 6 18:27:24 2023

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