Magnesium in PDB 6vgg: Crystal Structure of the Dna Binding Domains of Human Transcription Factor Erg, Human RUNX2 Bound to Core Binding Factor Beta (Cbfb), and Mithramycin, in Complex with 16MER Dna Cagaggatgtggcttc

The structure of Crystal Structure of the Dna Binding Domains of Human Transcription Factor Erg, Human RUNX2 Bound to Core Binding Factor Beta (Cbfb), and Mithramycin, in Complex with 16MER Dna Cagaggatgtggcttc, PDB code: 6vgg was solved by C.Hou, J.Rohr, O.V.Tsodikov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.00 / 4.31
Space group	P 62 2 2
Cell size a, b, c (Å), α, β, γ (°)	104.678, 104.678, 322.836, 90.00, 90.00, 120.00
R / Rfree (%)	25.1 / 28.5

The binding sites of Magnesium atom in the Crystal Structure of the Dna Binding Domains of Human Transcription Factor Erg, Human RUNX2 Bound to Core Binding Factor Beta (Cbfb), and Mithramycin, in Complex with 16MER Dna Cagaggatgtggcttc (pdb code 6vgg). 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 the Dna Binding Domains of Human Transcription Factor Erg, Human RUNX2 Bound to Core Binding Factor Beta (Cbfb), and Mithramycin, in Complex with 16MER Dna Cagaggatgtggcttc, PDB code: 6vgg:

Magnesium binding site 1 out of 1 in the Crystal Structure of the Dna Binding Domains of Human Transcription Factor Erg, Human RUNX2 Bound to Core Binding Factor Beta (Cbfb), and Mithramycin, in Complex with 16MER Dna Cagaggatgtggcttc


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 the Dna Binding Domains of Human Transcription Factor Erg, Human RUNX2 Bound to Core Binding Factor Beta (Cbfb), and Mithramycin, in Complex with 16MER Dna Cagaggatgtggcttc within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg102 b:1.0 occ:1.00 OBR C:QWP101 2.2 0.2 1.0 OBU C:QWP101 2.2 0.1 1.0 O B:HOH201 2.2 1.0 1.0 OBU B:QWP101 2.2 0.8 1.0 OBR B:QWP101 2.2 0.2 1.0 O C:HOH201 2.6 0.7 1.0 CBQ C:QWP101 3.3 0.7 1.0 CBQ B:QWP101 3.3 0.1 1.0 CBT C:QWP101 3.3 0.0 1.0 CBT B:QWP101 3.4 0.0 1.0 N2 B:DG6 3.6 0.1 1.0 CBS C:QWP101 3.8 0.3 1.0 CBS B:QWP101 3.8 0.8 1.0 N3 B:DG6 3.9 0.7 1.0 OCB C:QWP101 4.1 0.7 1.0 OCB B:QWP101 4.2 0.1 1.0 C2 B:DG6 4.2 0.2 1.0 CBD C:QWP101 4.4 0.1 1.0 CBD B:QWP101 4.5 0.6 1.0 CBZ C:QWP101 4.5 0.4 1.0 OBC B:QWP101 4.5 0.0 1.0 CBZ B:QWP101 4.5 0.9 1.0 CAV B:QWP101 4.6 0.1 1.0 OBC C:QWP101 4.6 0.2 1.0 CBB B:QWP101 4.7 0.5 1.0 O4' B:DA7 4.7 0.6 1.0 O2 C:DC13 4.8 0.2 1.0 CBB C:QWP101 4.8 0.2 1.0 O4' C:DT14 4.8 0.2 1.0 CCA C:QWP101 4.8 0.9 1.0 CCA B:QWP101 4.9 0.1 1.0 C5' C:DT14 4.9 0.8 1.0

C.Hou, P.Mitra, J.Rohr, O.V.Tsodikov. Allosteric Interference in Oncogenic FLI1 and Erg Transactions By Mithramycins Structure 2020.
ISSN: ISSN 0969-2126