Manganese in PDB 4m0a: Human Dna Polymerase Mu Post-Catalytic Complex

All present enzymatic activity of Human Dna Polymerase Mu Post-Catalytic Complex:
2.7.7.7;

The structure of Human Dna Polymerase Mu Post-Catalytic Complex, PDB code: 4m0a was solved by A.F.Moon, J.M.Pryor, D.A.Ramsden, T.A.Kunkel, K.Bebenek, L.C.Pedersen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.38 / 1.85
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	60.018, 68.670, 110.444, 90.00, 90.00, 90.00
R / Rfree (%)	16.3 / 20

The structure of Human Dna Polymerase Mu Post-Catalytic Complex also contains other interesting chemical elements:

Magnesium

(Mg)

3 atoms

The binding sites of Manganese atom in the Human Dna Polymerase Mu Post-Catalytic Complex (pdb code 4m0a). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Human Dna Polymerase Mu Post-Catalytic Complex, PDB code: 4m0a:

Manganese binding site 1 out of 1 in the Human Dna Polymerase Mu Post-Catalytic Complex


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Human Dna Polymerase Mu Post-Catalytic Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn505 b:15.4 occ:1.00 OD1 A:ASP332 2.0 4.9 1.0 OD1 A:ASP330 2.0 10.5 0.5 OD1 A:ASP418 2.2 5.0 1.0 OP1 P:DT5 2.3 3.2 1.0 OD1 A:ASP330 2.7 6.6 0.5 CG A:ASP330 2.7 8.5 0.5 OD2 A:ASP330 2.8 6.8 0.5 O3' P:DA4 2.8 4.3 1.0 CG A:ASP332 2.9 4.4 1.0 O P:HOH208 3.0 13.9 1.0 P P:DT5 3.1 4.4 1.0 CG A:ASP418 3.2 8.1 1.0 OD2 A:ASP332 3.2 4.7 1.0 MG A:MG501 3.3 5.6 1.0 CG A:ASP330 3.4 8.0 0.5 CB A:ASP418 3.8 2.7 1.0 CB A:ASP330 4.0 6.0 0.5 C3' P:DA4 4.1 2.4 1.0 C5' P:DA4 4.1 6.6 1.0 C4' P:DA4 4.1 4.0 1.0 CB A:ASP330 4.1 5.9 0.5 OD2 A:ASP330 4.2 8.2 0.5 OD2 A:ASP418 4.2 7.4 1.0 OP2 P:DT5 4.2 4.6 1.0 O5' P:DT5 4.3 2.3 1.0 CB A:ASP332 4.3 2.2 1.0 C5' P:DT5 4.3 1.5 1.0 O A:VAL331 4.6 2.8 1.0 CZ3 A:TRP434 4.7 3.6 1.0 NH2 A:ARG416 4.7 4.1 1.0 CA A:ASP332 4.7 3.1 1.0 C A:VAL331 4.8 4.3 1.0 N A:ASP418 4.8 2.3 1.0 O A:HOH900 4.9 13.4 1.0 O A:HOH601 4.9 7.9 1.0 N A:ASP332 4.9 2.1 1.0 CA A:ASP418 5.0 3.5 1.0

A.F.Moon, J.M.Pryor, D.A.Ramsden, T.A.Kunkel, K.Bebenek, L.C.Pedersen. Sustained Active Site Rigidity During Synthesis By Human Dna Polymerase Mu. Nat.Struct.Mol.Biol. V. 21 253 2014.
ISSN: ISSN 1545-9993
PubMed: 24487959
DOI: 10.1038/NSMB.2766