Magnesium in PDB 1vaq: Crystal Structure of the MG2+-(Chromomycin A3)2-D(Ttggccaa)2 Complex Reveals Ggcc Binding Specificity of the Drug Dimer Chelated By Metal Ion

The structure of Crystal Structure of the MG2+-(Chromomycin A3)2-D(Ttggccaa)2 Complex Reveals Ggcc Binding Specificity of the Drug Dimer Chelated By Metal Ion, PDB code: 1vaq was solved by M.H.Hou, H.Robinson, Y.G.Gao, A.H.-J.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.00
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	42.230, 42.230, 246.110, 90.00, 90.00, 120.00
R / Rfree (%)	23.5 / 27.8

The binding sites of Magnesium atom in the Crystal Structure of the MG2+-(Chromomycin A3)2-D(Ttggccaa)2 Complex Reveals Ggcc Binding Specificity of the Drug Dimer Chelated By Metal Ion (pdb code 1vaq). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the MG2+-(Chromomycin A3)2-D(Ttggccaa)2 Complex Reveals Ggcc Binding Specificity of the Drug Dimer Chelated By Metal Ion, PDB code: 1vaq:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of the MG2+-(Chromomycin A3)2-D(Ttggccaa)2 Complex Reveals Ggcc Binding Specificity of the Drug Dimer Chelated By Metal Ion


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 MG2+-(Chromomycin A3)2-D(Ttggccaa)2 Complex Reveals Ggcc Binding Specificity of the Drug Dimer Chelated By Metal Ion within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg81 b:5.9 occ:1.00 O9 B:CPH23 1.8 3.5 1.0 O9 A:CPH33 1.9 11.2 1.0 O1 B:CPH23 2.0 8.7 1.0 O1 A:CPH33 2.0 14.4 1.0 O A:HOH481 2.1 4.4 1.0 O B:HOH480 2.1 1.7 1.0 C9 B:CPH23 3.0 1.7 1.0 C9 A:CPH33 3.0 13.3 1.0 C1 B:CPH23 3.0 5.2 1.0 C1 A:CPH33 3.1 16.4 1.0 C9A B:CPH23 3.4 4.3 1.0 C9A A:CPH33 3.4 9.1 1.0 O8 B:CPH23 3.9 11.5 1.0 O8 A:CPH33 3.9 14.3 1.0 O2 A:DC5 4.2 8.0 1.0 C8A B:CPH23 4.2 14.8 1.0 C8A A:CPH33 4.3 11.8 1.0 O4' A:DC6 4.3 20.4 1.0 C2 B:CPH23 4.4 6.4 1.0 C2 A:CPH33 4.4 16.3 1.0 O2 B:DC13 4.5 6.6 1.0 C1 B:CDR34 4.5 11.9 1.0 OGL B:CDR24 4.5 12.2 1.0 OGL B:CDR34 4.5 13.0 1.0 C8 B:CPH23 4.6 7.2 1.0 C8 A:CPH33 4.6 6.4 1.0 C1 B:CDR24 4.7 3.9 1.0 O4' B:DC14 4.7 11.6 1.0 C1' A:DC5 4.7 14.4 1.0 C2 B:CDR34 4.8 1.7 1.0 C4' A:DC6 4.9 19.0 1.0 C4A A:CPH33 4.9 8.6 1.0 C4A B:CPH23 4.9 9.9 1.0 C1' B:DC13 4.9 10.8 1.0 C6 C:CDR74 4.9 8.7 1.0 C5' A:DC6 5.0 5.9 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of the MG2+-(Chromomycin A3)2-D(Ttggccaa)2 Complex Reveals Ggcc Binding Specificity of the Drug Dimer Chelated By Metal Ion


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the MG2+-(Chromomycin A3)2-D(Ttggccaa)2 Complex Reveals Ggcc Binding Specificity of the Drug Dimer Chelated By Metal Ion within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg82 b:9.1 occ:1.00 O9 D:CPH63 1.8 4.4 1.0 O9 C:CPH73 1.9 12.1 1.0 O D:HOH483 2.0 2.3 1.0 O1 C:CPH73 2.1 10.6 1.0 O D:HOH482 2.1 21.1 1.0 O1 D:CPH63 2.1 10.4 1.0 C9 D:CPH63 3.0 5.4 1.0 C9 C:CPH73 3.1 8.2 1.0 C1 D:CPH63 3.1 12.5 1.0 C1 C:CPH73 3.1 16.3 1.0 C9A D:CPH63 3.4 3.0 1.0 C9A C:CPH73 3.5 13.3 1.0 O8 D:CPH63 3.8 17.2 1.0 O8 C:CPH73 4.0 7.4 1.0 C8A D:CPH63 4.2 14.1 1.0 O C:HOH230 4.2 37.3 1.0 C8A C:CPH73 4.3 17.5 1.0 O2 D:DC53 4.3 4.5 1.0 O2 C:DC45 4.4 12.9 1.0 C2 D:CPH63 4.5 5.6 1.0 C2 C:CPH73 4.5 10.4 1.0 O4' D:DC54 4.5 16.9 1.0 C8 D:CPH63 4.5 12.9 1.0 OGL D:CDR64 4.5 1.7 1.0 C1 D:CDR64 4.6 12.1 1.0 OGL C:CDR74 4.6 9.1 1.0 C1 C:CDR74 4.7 3.7 1.0 C8 C:CPH73 4.7 12.6 1.0 O4' C:DC46 4.7 6.2 1.0 C1' D:DC53 4.8 14.9 1.0 C4A D:CPH63 4.9 14.6 1.0 C2 D:CDR64 4.9 11.4 1.0 C4A C:CPH73 5.0 7.5 1.0

M.H.Hou, H.Robinson, Y.G.Gao, A.H.-J.Wang. Crystal Structure of the [MG2+-(Chromomycin A3)2]-D(Ttggccaa)2 Complex Reveals Ggcc Binding Specificity of the Drug Dimer Chelated By A Metal Ion Nucleic Acids Res. V. 32 2214 2004.
ISSN: ISSN 0305-1048
PubMed: 15107489
DOI: 10.1093/NAR/GKH549