Magnesium in PDB 1xhx: PHI29 Dna Polymerase, Orthorhombic Crystal Form

All present enzymatic activity of PHI29 Dna Polymerase, Orthorhombic Crystal Form:
2.7.7.7;

The structure of PHI29 Dna Polymerase, Orthorhombic Crystal Form, PDB code: 1xhx was solved by S.Kamtekar, A.J.Berman, J.Wang, J.M.Lazaro, M.De Vega, L.Blanco, M.Salas, T.A.Steitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.96 / 2.35
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	96.256, 149.911, 199.024, 90.00, 90.00, 90.00
R / Rfree (%)	20.6 / 25.7

The binding sites of Magnesium atom in the PHI29 Dna Polymerase, Orthorhombic Crystal Form (pdb code 1xhx). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the PHI29 Dna Polymerase, Orthorhombic Crystal Form, PDB code: 1xhx:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the PHI29 Dna Polymerase, Orthorhombic Crystal Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of PHI29 Dna Polymerase, Orthorhombic Crystal Form within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg5000 b:47.9 occ:1.00 OD1 C:ASP523 2.4 41.2 1.0 O C:HOH5370 2.5 55.8 1.0 O C:HOH5371 2.5 43.9 1.0 O C:HOH5372 2.5 46.2 1.0 O C:HOH5374 2.5 40.9 1.0 O C:HOH5373 2.5 41.8 1.0 CG C:ASP523 3.3 44.8 1.0 OD2 C:ASP523 3.5 32.0 1.0 O C:THR522 4.3 34.5 1.0 O C:HOH5181 4.4 36.7 1.0 CB C:ASP523 4.7 37.6 1.0 O C:HOH5183 4.8 42.8 1.0 OE2 C:GLU508 4.9 81.0 1.0

Magnesium binding site 2 out of 2 in the PHI29 Dna Polymerase, Orthorhombic Crystal Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of PHI29 Dna Polymerase, Orthorhombic Crystal Form within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg5001 b:53.8 occ:1.00 O C:HOH5377 2.4 42.5 1.0 O C:HOH5379 2.4 53.6 1.0 O C:HOH5375 2.4 55.1 1.0 O C:HOH5378 2.5 52.0 1.0 O C:HOH5376 2.5 49.0 1.0 OD1 C:ASP503 4.0 45.8 1.0 OD2 C:ASP503 4.2 36.2 1.0 O C:HOH5320 4.4 44.4 1.0 CG C:ASP503 4.4 44.2 1.0 CB C:PHE526 4.6 29.2 1.0 O C:HOH5191 4.7 47.0 1.0 O C:ILE524 4.7 30.5 1.0 NH2 C:ARG491 4.8 32.8 1.0

S.Kamtekar, A.J.Berman, J.Wang, J.M.Lazaro, M.De Vega, L.Blanco, M.Salas, T.A.Steitz. Insights Into Strand Displacement and Processivity From the Crystal Structure of the Protein-Primed Dna Polymerase of Bacteriophage PHI29 Mol.Cell V. 16 609 2004.
ISSN: ISSN 1097-2765
PubMed: 15546620
DOI: 10.1016/J.MOLCEL.2004.10.019