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Magnesium in PDB 2o8e: Human Mutsalpha (MSH2/MSH6) Bound to A G T Mispair, with Adp Bound to MSH2 Only

Protein crystallography data

The structure of Human Mutsalpha (MSH2/MSH6) Bound to A G T Mispair, with Adp Bound to MSH2 Only, PDB code: 2o8e was solved by J.J.Warren, T.J.Pohlhaus, A.Changela, P.L.Modrich, L.S.Beese, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 3.30
Space group P 43 3 2
Cell size a, b, c (Å), α, β, γ (°) 257.510, 257.510, 257.510, 90.00, 90.00, 90.00
R / Rfree (%) 25.3 / 29.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Human Mutsalpha (MSH2/MSH6) Bound to A G T Mispair, with Adp Bound to MSH2 Only (pdb code 2o8e). 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 Human Mutsalpha (MSH2/MSH6) Bound to A G T Mispair, with Adp Bound to MSH2 Only, PDB code: 2o8e:

Magnesium binding site 1 out of 1 in 2o8e

Go back to Magnesium Binding Sites List in 2o8e
Magnesium binding site 1 out of 1 in the Human Mutsalpha (MSH2/MSH6) Bound to A G T Mispair, with Adp Bound to MSH2 Only


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Mutsalpha (MSH2/MSH6) Bound to A G T Mispair, with Adp Bound to MSH2 Only within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg935

b:79.0
occ:1.00
OG A:SER676 2.5 99.9 1.0
O1B A:ADP936 2.6 0.5 1.0
O2B A:ADP936 2.7 0.8 1.0
PB A:ADP936 3.1 0.9 1.0
CB A:SER676 3.5 0.2 1.0
O2A A:ADP936 3.5 0.3 1.0
OD1 A:ASP748 4.1 0.7 1.0
O3A A:ADP936 4.3 0.4 1.0
O3B A:ADP936 4.3 0.4 1.0
OD2 A:ASP748 4.4 0.8 1.0
PA A:ADP936 4.5 100.0 1.0
N A:SER676 4.5 0.5 1.0
OE2 A:GLU749 4.6 0.8 1.0
CA A:SER676 4.6 0.2 1.0
CG A:ASP748 4.7 0.8 1.0

Reference:

J.J.Warren, T.J.Pohlhaus, A.Changela, R.R.Iyer, P.L.Modrich, L.S.Beese. Structure of the Human Mutsalpha Dna Lesion Recognition Complex. Mol.Cell V. 26 579 2007.
ISSN: ISSN 1097-2765
PubMed: 17531815
DOI: 10.1016/J.MOLCEL.2007.04.018
Page generated: Wed Aug 14 01:23:54 2024

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