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Magnesium in PDB 3qf7: The MRE11:RAD50 Complex Forms An Atp Dependent Molecular Clamp in Dna Double-Strand Break Repair

Protein crystallography data

The structure of The MRE11:RAD50 Complex Forms An Atp Dependent Molecular Clamp in Dna Double-Strand Break Repair, PDB code: 3qf7 was solved by C.Moeckel, K.Lammens, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.17 / 1.90
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 49.149, 68.400, 71.111, 98.64, 111.14, 92.03
R / Rfree (%) 15.7 / 19.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The MRE11:RAD50 Complex Forms An Atp Dependent Molecular Clamp in Dna Double-Strand Break Repair (pdb code 3qf7). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The MRE11:RAD50 Complex Forms An Atp Dependent Molecular Clamp in Dna Double-Strand Break Repair, PDB code: 3qf7:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3qf7

Go back to Magnesium Binding Sites List in 3qf7
Magnesium binding site 1 out of 2 in the The MRE11:RAD50 Complex Forms An Atp Dependent Molecular Clamp in Dna Double-Strand Break Repair


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The MRE11:RAD50 Complex Forms An Atp Dependent Molecular Clamp in Dna Double-Strand Break Repair within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg854

b:13.6
occ:1.00
O1G A:ANP853 2.1 12.2 1.0
O2B A:ANP853 2.1 11.3 1.0
OE1 A:GLN142 2.1 12.5 1.0
O A:HOH863 2.2 9.9 1.0
OG A:SER37 2.2 11.2 1.0
O A:HOH876 2.2 11.7 1.0
CB A:SER37 3.1 12.8 1.0
CD A:GLN142 3.1 16.4 1.0
PB A:ANP853 3.3 12.5 1.0
PG A:ANP853 3.3 13.6 1.0
NE2 A:GLN142 3.5 12.1 1.0
N3B A:ANP853 3.7 14.4 1.0
O2A A:ANP853 3.9 14.5 1.0
N A:SER37 4.0 11.7 1.0
O3G A:ANP853 4.1 13.5 1.0
O A:HOH896 4.1 19.2 1.0
OD1 A:ASP797 4.1 12.9 1.0
OD2 A:ASP797 4.1 11.6 1.0
CA A:SER37 4.1 11.0 1.0
O3A A:ANP853 4.1 10.2 1.0
OE2 A:GLU798 4.2 7.8 0.3
N B:GLY769 4.3 11.1 1.0
CD A:GLU798 4.4 20.0 0.3
O2G A:ANP853 4.4 13.6 1.0
CG A:GLN142 4.4 12.5 1.0
O1B A:ANP853 4.5 13.4 1.0
PA A:ANP853 4.6 13.3 1.0
CG A:ASP797 4.6 10.3 1.0
CB A:GLN142 4.6 10.4 1.0
OE1 A:GLU798 4.6 25.9 0.3
CB B:SER768 4.7 14.2 1.0
CG A:GLU798 4.9 15.5 0.3
NZ A:LYS36 5.0 18.0 1.0
CE A:LYS36 5.0 17.4 1.0

Magnesium binding site 2 out of 2 in 3qf7

Go back to Magnesium Binding Sites List in 3qf7
Magnesium binding site 2 out of 2 in the The MRE11:RAD50 Complex Forms An Atp Dependent Molecular Clamp in Dna Double-Strand Break Repair


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The MRE11:RAD50 Complex Forms An Atp Dependent Molecular Clamp in Dna Double-Strand Break Repair within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg854

b:14.2
occ:1.00
O3G B:ANP853 2.1 13.6 1.0
OE1 B:GLN142 2.1 12.9 1.0
O2B B:ANP853 2.2 11.6 1.0
OG B:SER37 2.2 10.9 1.0
O B:HOH856 2.2 11.3 1.0
O B:HOH855 2.2 12.2 1.0
CD B:GLN142 3.1 13.6 1.0
CB B:SER37 3.2 10.7 1.0
PG B:ANP853 3.2 15.4 1.0
PB B:ANP853 3.3 13.2 1.0
NE2 B:GLN142 3.5 12.9 1.0
N3B B:ANP853 3.7 13.3 1.0
N B:SER37 4.0 14.1 1.0
O2A B:ANP853 4.1 14.3 1.0
OD2 B:ASP797 4.1 12.3 1.0
CA B:SER37 4.2 11.7 1.0
O3A B:ANP853 4.2 12.2 1.0
OD1 B:ASP797 4.2 12.5 1.0
O2G B:ANP853 4.2 13.2 1.0
O A:HOH867 4.3 17.7 1.0
N A:GLY769 4.3 13.6 1.0
O1G B:ANP853 4.3 14.6 1.0
OE2 B:GLU798 4.4 20.1 1.0
CG B:GLN142 4.4 13.3 1.0
O1B B:ANP853 4.5 13.0 1.0
CG B:ASP797 4.6 11.9 1.0
CG B:GLU798 4.6 26.4 1.0
CB B:GLN142 4.6 9.9 1.0
PA B:ANP853 4.6 13.4 1.0
CE B:LYS36 4.7 12.3 1.0
CB A:SER768 4.8 14.1 1.0
CB B:LYS36 4.9 12.7 1.0
CA A:GLY769 4.9 15.3 1.0
CD B:GLU798 5.0 26.9 1.0
O A:HOH882 5.0 18.4 1.0

Reference:

K.Lammens, D.J.Bemeleit, C.Moeckel, E.Clausing, A.Schele, S.Hartung, C.B.Schiller, M.Lucas, C.Angermueller, J.Soeding, K.Straesser, K.P.Hopfner. The MRE11:RAD50 Structure Shows An Atp-Dependent Molecular Clamp in Dna Double-Strand Break Repair. Cell(Cambridge,Mass.) V. 145 54 2011.
ISSN: ISSN 0092-8674
PubMed: 21458667
DOI: 10.1016/J.CELL.2011.02.038
Page generated: Thu Aug 15 10:02:31 2024

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