Magnesium in PDB 6pl7: Structure of Human Dna Polymerase Eta Complexed with A in the Template Base Paired with Incoming Non-Hydrolyzable Ttp

All present enzymatic activity of Structure of Human Dna Polymerase Eta Complexed with A in the Template Base Paired with Incoming Non-Hydrolyzable Ttp:
2.7.7.7;

The structure of Structure of Human Dna Polymerase Eta Complexed with A in the Template Base Paired with Incoming Non-Hydrolyzable Ttp, PDB code: 6pl7 was solved by M.C.Koag, S.Lee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.70 / 2.50
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	98.700, 98.700, 82.447, 90.00, 90.00, 120.00
R / Rfree (%)	21 / 28.1

The binding sites of Magnesium atom in the Structure of Human Dna Polymerase Eta Complexed with A in the Template Base Paired with Incoming Non-Hydrolyzable Ttp (pdb code 6pl7). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Human Dna Polymerase Eta Complexed with A in the Template Base Paired with Incoming Non-Hydrolyzable Ttp, PDB code: 6pl7:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of Human Dna Polymerase Eta Complexed with A in the Template Base Paired with Incoming Non-Hydrolyzable Ttp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Human Dna Polymerase Eta Complexed with A in the Template Base Paired with Incoming Non-Hydrolyzable Ttp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:23.3 occ:1.00 O2B A:1FZ501 2.0 23.8 1.0 O A:MET14 2.0 19.0 1.0 O1A A:1FZ501 2.1 24.6 1.0 O2G A:1FZ501 2.1 25.5 1.0 OD2 A:ASP13 2.2 19.6 1.0 OD2 A:ASP115 2.4 22.7 1.0 PB A:1FZ501 3.0 23.4 1.0 PG A:1FZ501 3.2 27.8 1.0 C A:MET14 3.2 19.8 1.0 CG A:ASP13 3.3 20.8 1.0 PA A:1FZ501 3.3 24.8 1.0 O3B A:1FZ501 3.4 26.0 1.0 CG A:ASP115 3.5 22.9 1.0 N3A A:1FZ501 3.6 24.2 1.0 MG A:MG503 3.7 23.0 1.0 O1G A:1FZ501 3.7 29.3 1.0 OD1 A:ASP13 3.8 22.0 1.0 N A:MET14 3.9 20.3 1.0 NZ A:LYS231 4.0 23.3 1.0 CA A:MET14 4.1 19.9 1.0 OD1 A:ASP115 4.1 23.4 1.0 N A:ASP15 4.2 18.2 1.0 O5' A:1FZ501 4.2 23.8 1.0 C A:ASP13 4.3 20.9 1.0 C5' A:1FZ501 4.3 22.6 1.0 N A:CYS16 4.3 17.3 1.0 CA A:ASP15 4.3 19.3 1.0 CB A:ASP13 4.4 21.3 1.0 O1B A:1FZ501 4.4 22.6 1.0 O3G A:1FZ501 4.5 30.7 1.0 C A:ASP15 4.5 19.1 1.0 CB A:ASP115 4.5 21.0 1.0 CB A:MET14 4.5 19.5 1.0 O2A A:1FZ501 4.6 26.7 1.0 O A:ASP13 4.6 20.7 1.0 N A:PHE17 4.7 18.0 1.0 CE A:LYS231 4.8 25.1 1.0 CA A:ASP13 4.8 21.7 1.0 O A:ASP115 4.8 18.6 1.0 CB A:PHE17 4.9 17.4 1.0

Magnesium binding site 2 out of 2 in the Structure of Human Dna Polymerase Eta Complexed with A in the Template Base Paired with Incoming Non-Hydrolyzable Ttp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Human Dna Polymerase Eta Complexed with A in the Template Base Paired with Incoming Non-Hydrolyzable Ttp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg503 b:23.0 occ:1.00 O1A A:1FZ501 2.2 24.6 1.0 OE1 A:GLU116 2.2 21.9 1.0 OD1 A:ASP13 2.3 22.0 1.0 O3' P:DT8 2.4 20.8 1.0 OD1 A:ASP115 2.5 23.4 1.0 PA A:1FZ501 3.0 24.8 1.0 OD2 A:ASP115 3.1 22.7 1.0 CG A:ASP115 3.2 22.9 1.0 C3' P:DT8 3.2 23.6 1.0 O2A A:1FZ501 3.2 26.7 1.0 CG A:ASP13 3.2 20.8 1.0 CD A:GLU116 3.3 22.2 1.0 OD2 A:ASP13 3.4 19.6 1.0 O5' A:1FZ501 3.7 23.8 1.0 MG A:MG502 3.7 23.3 1.0 OE2 A:GLU116 4.0 22.2 1.0 OG A:SER113 4.2 19.3 1.0 NZ A:LYS224 4.2 18.0 1.0 C4' P:DT8 4.2 25.8 1.0 C5' A:1FZ501 4.3 22.6 1.0 CB A:GLU116 4.3 20.6 1.0 C2' P:DT8 4.3 23.7 1.0 CG A:GLU116 4.4 20.8 1.0 O2G A:1FZ501 4.5 25.5 1.0 N3A A:1FZ501 4.5 24.2 1.0 CB A:ASP13 4.6 21.3 1.0 CB A:ASP115 4.6 21.0 1.0 O5' P:DT8 4.7 43.8 1.0 O2B A:1FZ501 4.8 23.8 1.0 O A:ASP115 4.8 18.6 1.0 C5' P:DT8 4.8 30.9 1.0 C A:ASP115 4.9 18.5 1.0

M.C.Koag, S.Lee. Structure of Human Dna Polymerase Eta Complexed with A in the Template Base Paired with Incoming Non-Hydrolyzable Ttp To Be Published.