Manganese in PDB 8q44: Crystal Structure of CA4-Bound CAN2 (E364R) in Complex with Oligo-T Dna

The structure of Crystal Structure of CA4-Bound CAN2 (E364R) in Complex with Oligo-T Dna, PDB code: 8q44 was solved by K.Jungfer, A.Sigg, M.Jinek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	57.46 / 2.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	57.714, 78.357, 94.661, 90, 95.35, 90
R / Rfree (%)	19.8 / 22.6

The binding sites of Manganese atom in the Crystal Structure of CA4-Bound CAN2 (E364R) in Complex with Oligo-T Dna (pdb code 8q44). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystal Structure of CA4-Bound CAN2 (E364R) in Complex with Oligo-T Dna, PDB code: 8q44:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Crystal Structure of CA4-Bound CAN2 (E364R) in Complex with Oligo-T Dna


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of CA4-Bound CAN2 (E364R) in Complex with Oligo-T Dna within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn501 b:71.4 occ:0.00 O A:HOH601 1.9 71.0 1.0 OD2 A:ASP343 2.2 59.6 1.0 O C:HOH102 2.2 82.2 1.0 O A:HOH608 2.2 91.2 1.0 O A:HOH626 2.5 62.0 1.0 O A:LEU357 2.5 61.2 1.0 CG A:ASP343 3.1 53.7 1.0 OD1 A:ASP343 3.2 58.0 1.0 C A:LEU357 3.6 55.0 1.0 OE2 A:GLU304 3.6 68.5 1.0 NZ A:LYS369 3.8 89.6 1.0 O5' C:DT1 3.9 148.4 1.0 N A:LEU357 3.9 52.0 1.0 CA A:LEU357 4.2 52.9 1.0 OP2 C:DT1 4.3 148.6 1.0 CB A:LEU357 4.4 51.1 1.0 C5' C:DT1 4.4 146.7 1.0 CB A:ASP343 4.4 48.4 1.0 CE A:LYS369 4.6 72.4 1.0 CD A:GLU304 4.6 64.0 1.0 OG A:SER356 4.6 50.0 1.0 O C:HOH101 4.6 61.9 1.0 P C:DT1 4.7 163.3 1.0 N A:THR358 4.7 60.8 1.0 O A:HOH633 4.8 48.6 1.0 CG A:GLU304 4.8 60.0 1.0 OP2 C:DT2 4.9 142.0 1.0

Manganese binding site 2 out of 4 in the Crystal Structure of CA4-Bound CAN2 (E364R) in Complex with Oligo-T Dna


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of CA4-Bound CAN2 (E364R) in Complex with Oligo-T Dna within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn502 b:94.5 occ:1.00 OE2 B:GLU76 2.6 83.1 1.0 OE1 A:GLU142 3.1 62.2 1.0 OE2 A:GLU142 3.2 73.2 1.0 CD B:GLU76 3.6 77.1 1.0 CD A:GLU142 3.6 66.4 1.0 CG B:GLU76 4.2 68.5 1.0 OE1 B:GLU76 4.5 74.2 1.0

Manganese binding site 3 out of 4 in the Crystal Structure of CA4-Bound CAN2 (E364R) in Complex with Oligo-T Dna


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of CA4-Bound CAN2 (E364R) in Complex with Oligo-T Dna within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn501 b:65.1 occ:1.00 NE2 B:HIS168 2.0 77.9 1.0 OD1 B:ASP166 2.4 61.7 1.0 CE1 B:HIS168 2.6 65.7 1.0 CD2 B:HIS168 3.2 70.6 1.0 CG B:ASP166 3.6 66.3 1.0 ND1 B:HIS168 3.9 67.2 1.0 OD2 B:ASP166 4.1 65.2 1.0 CG B:HIS168 4.2 72.1 1.0 CB B:ASP166 4.8 56.9 1.0 CA B:ASP166 4.8 58.5 1.0

Manganese binding site 4 out of 4 in the Crystal Structure of CA4-Bound CAN2 (E364R) in Complex with Oligo-T Dna


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of CA4-Bound CAN2 (E364R) in Complex with Oligo-T Dna within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn502 b:93.0 occ:1.00 OD2 B:ASP343 2.3 59.4 1.0 O B:LEU357 2.5 60.4 1.0 CG B:ASP343 3.3 54.4 1.0 C B:LEU357 3.6 51.5 1.0 OD1 B:ASP343 3.6 56.7 1.0 OE2 B:GLU304 3.7 55.0 1.0 N B:LEU357 3.8 50.5 1.0 CA B:LEU357 4.1 50.8 1.0 CB B:LEU357 4.4 51.2 1.0 O B:HOH655 4.4 50.3 1.0 OG B:SER356 4.4 54.9 1.0 CD B:GLU304 4.6 58.5 1.0 CB B:ASP343 4.6 49.4 1.0 N B:THR358 4.7 57.0 1.0 CG B:GLU304 4.8 50.8 1.0 O B:HOH652 4.9 45.5 1.0 C B:SER356 5.0 52.3 1.0

K.Jungfer, A.Sigg, M.Jinek. Substrate Selectivity and Catalytic Activation of the Type III Crispr-Associated Ancillary Nuclease CAN2 To Be Published.