Manganese in PDB 1ckn: Structure of Guanylylated Mrna Capping Enzyme Complexed with Gtp

All present enzymatic activity of Structure of Guanylylated Mrna Capping Enzyme Complexed with Gtp:
2.7.7.50;

The structure of Structure of Guanylylated Mrna Capping Enzyme Complexed with Gtp, PDB code: 1ckn was solved by K.Hakansson, A.J.Doherty, D.B.Wigley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.50
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	94.906, 212.953, 105.016, 90.00, 90.00, 90.00
R / Rfree (%)	22.4 / 29.9

The binding sites of Manganese atom in the Structure of Guanylylated Mrna Capping Enzyme Complexed with Gtp (pdb code 1ckn). 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 Structure of Guanylylated Mrna Capping Enzyme Complexed with Gtp, PDB code: 1ckn:

Manganese binding site 1 out of 1 in the Structure of Guanylylated Mrna Capping Enzyme Complexed with Gtp


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of Guanylylated Mrna Capping Enzyme Complexed with Gtp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn1001 b:28.2 occ:1.00 O B:HOH1163 2.3 25.9 1.0 O B:HOH1121 2.3 10.9 1.0 O1P B:GPL82 2.4 7.6 1.0 O B:HOH1122 2.4 22.1 1.0 O B:HOH1156 3.1 28.7 1.0 O B:HOH1114 3.1 19.0 1.0 O B:HOH1101 3.4 15.2 1.0 P B:GPL82 3.8 22.6 1.0 NZ B:GPL82 4.0 4.3 1.0 O B:HOH1119 4.3 23.9 1.0 OD2 B:ASP213 4.3 15.7 1.0 O2P B:GPL82 4.4 29.3 1.0 O B:GLY85 4.5 20.6 1.0 OD1 B:ASP84 4.6 10.6 1.0 C4' B:GPL82 4.6 13.4 1.0 O4' B:GPL82 4.7 14.9 1.0 O2' B:GPL82 4.7 21.8 1.0 OD1 B:ASP213 4.8 13.6 1.0 O B:THR83 4.8 18.8 1.0 O B:HOH1049 4.9 30.7 1.0 O5' B:GPL82 4.9 23.8 1.0 OE1 B:GLU131 4.9 24.6 1.0 CG B:ASP213 5.0 12.6 1.0

K.Hakansson, A.J.Doherty, S.Shuman, D.B.Wigley. X-Ray Crystallography Reveals A Large Conformational Change During Guanyl Transfer By Mrna Capping Enzymes. Cell(Cambridge,Mass.) V. 89 545 1997.
ISSN: ISSN 0092-8674
PubMed: 9160746
DOI: 10.1016/S0092-8674(00)80236-6