Manganese in PDB 3g0a: MTH0212 with Two Bound Manganese Ions

All present enzymatic activity of MTH0212 with Two Bound Manganese Ions:
3.1.11.2;

The structure of MTH0212 with Two Bound Manganese Ions, PDB code: 3g0a was solved by K.Lakomek, A.Dickmanns, R.Ficner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.83 / 2.60
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	56.381, 56.381, 162.932, 90.00, 90.00, 120.00
R / Rfree (%)	19 / 25.2

The binding sites of Manganese atom in the MTH0212 with Two Bound Manganese Ions (pdb code 3g0a). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the MTH0212 with Two Bound Manganese Ions, PDB code: 3g0a:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the MTH0212 with Two Bound Manganese Ions


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of MTH0212 with Two Bound Manganese Ions within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn266 b:73.7 occ:1.00 OD1 A:ASN153 2.3 28.0 1.0 O A:HOH321 2.6 24.1 1.0 OD1 A:ASP151 2.6 25.0 1.0 O A:HOH331 2.8 13.4 1.0 CG A:ASN153 3.3 25.9 1.0 CG A:ASP151 3.4 22.5 1.0 OD2 A:ASP151 3.5 20.6 1.0 NE2 A:HIS248 3.6 22.6 1.0 ND2 A:ASN153 3.7 25.9 1.0 O A:HOH334 3.9 21.9 1.0 CE1 A:HIS248 3.9 22.6 1.0 ND2 A:ASN10 4.1 21.7 1.0 ND2 A:ASN114 4.3 34.6 1.0 CD1 A:LEU221 4.4 19.6 1.0 CE1 A:TYR111 4.5 25.1 1.0 CB A:ASN153 4.7 24.8 1.0 CB A:ASP151 4.8 22.6 1.0 CD2 A:HIS248 4.8 22.4 1.0 OH A:TYR111 4.8 25.2 1.0 OE1 A:GLU38 4.9 29.3 1.0 CA A:ASN153 5.0 24.7 1.0

Manganese binding site 2 out of 2 in the MTH0212 with Two Bound Manganese Ions


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of MTH0212 with Two Bound Manganese Ions within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn267 b:33.8 occ:1.00 ND2 A:ASN12 2.2 23.0 1.0 OE2 A:GLU38 2.4 31.2 1.0 OE1 A:GLU38 2.5 29.3 1.0 O A:HOH318 2.7 26.5 1.0 CD A:GLU38 2.8 29.3 1.0 CG A:ASN12 3.2 25.0 1.0 CB A:ASN12 3.7 24.9 1.0 CA A:ASN12 3.9 25.2 1.0 OD2 A:ASP247 4.2 27.3 1.0 OD1 A:ASN10 4.2 23.2 1.0 OD1 A:ASN12 4.2 25.2 1.0 O A:HOH339 4.2 43.3 1.0 CG A:GLU38 4.3 28.3 1.0 OD1 A:ASP247 4.4 26.8 1.0 NZ A:LYS40 4.5 27.2 1.0 CG A:ASP247 4.7 27.5 1.0 N A:ASN12 4.8 25.8 1.0 O A:HOH321 4.9 24.1 1.0 O A:HOH340 4.9 20.6 1.0 C A:ASN12 4.9 24.8 1.0 CB A:GLU38 5.0 27.2 1.0

K.Lakomek, A.Dickmanns, E.Ciirdaeva, L.Schomacher, R.Ficner. Crystal Structure Analysis of Dna Uridine Endonuclease MTH212 Bound to Dna J.Mol.Biol. V. 399 604 2010.
ISSN: ISSN 0022-2836
PubMed: 20434457
DOI: 10.1016/J.JMB.2010.04.044