Cobalt in PDB 3r61: Structure of the Mntr CO2+ Complex

The structure of Structure of the Mntr CO2+ Complex, PDB code: 3r61 was solved by A.Glasfeld, M.B.Brophy, J.I.Kliegman, S.L.Griner, J.C.Nix, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.45 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.930, 75.013, 96.166, 90.00, 90.00, 90.00
R / Rfree (%)	21.4 / 25.8

The binding sites of Cobalt atom in the Structure of the Mntr CO2+ Complex (pdb code 3r61). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Structure of the Mntr CO2+ Complex, PDB code: 3r61:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Structure of the Mntr CO2+ Complex


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Structure of the Mntr CO2+ Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Co1 b:25.4 occ:1.00 ND1 A:HIS77 2.1 24.2 1.0 OE2 A:GLU11 2.1 30.2 1.0 OE2 A:GLU99 2.2 51.5 1.0 OE2 A:GLU102 2.3 30.1 1.0 OE1 A:GLU102 2.3 29.1 1.0 O A:HOH143 2.4 46.0 1.0 CD A:GLU102 2.6 26.6 1.0 CD A:GLU11 2.9 32.5 1.0 OE1 A:GLU11 3.0 30.9 1.0 CE1 A:HIS77 3.0 21.4 1.0 CG A:HIS77 3.1 25.2 1.0 CD A:GLU99 3.3 45.2 1.0 CB A:HIS77 3.4 23.4 1.0 OE1 A:GLU99 3.7 49.2 1.0 O A:HOH149 4.1 23.2 1.0 O A:HOH197 4.1 32.4 1.0 CG A:GLU102 4.1 20.2 1.0 NE2 A:HIS77 4.1 26.9 1.0 CD2 A:HIS77 4.2 22.9 1.0 O A:HOH162 4.2 38.8 1.0 CG A:GLU11 4.3 35.2 1.0 O A:HOH201 4.3 50.4 1.0 O A:HOH194 4.3 50.0 1.0 CA A:HIS77 4.5 25.7 1.0 CG A:GLU99 4.6 27.7 1.0 CG1 A:VAL98 4.6 20.1 1.0 CA A:GLU99 4.8 20.8 1.0 CB A:GLU102 4.9 19.3 1.0

Cobalt binding site 2 out of 2 in the Structure of the Mntr CO2+ Complex


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Structure of the Mntr CO2+ Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Co143 b:23.9 occ:1.00 ND1 B:HIS77 1.9 21.1 1.0 OE2 B:GLU11 2.0 28.3 1.0 O B:HOH144 2.2 35.0 1.0 OE2 B:GLU102 2.2 32.4 1.0 OE2 B:GLU99 2.4 56.9 1.0 OE1 B:GLU102 2.4 22.0 1.0 CD B:GLU102 2.6 26.2 1.0 CD B:GLU11 2.7 32.0 1.0 CE1 B:HIS77 2.8 28.7 1.0 OE1 B:GLU11 2.8 32.8 1.0 CG B:HIS77 3.1 23.9 1.0 CD B:GLU99 3.5 54.8 1.0 CB B:HIS77 3.6 18.3 1.0 OE1 B:GLU99 3.9 59.9 1.0 NE2 B:HIS77 4.0 25.5 1.0 CD2 B:HIS77 4.1 23.4 1.0 CG B:GLU102 4.1 17.5 1.0 O B:HOH162 4.2 36.3 1.0 O B:HOH153 4.2 23.2 1.0 CG B:GLU11 4.2 25.6 1.0 O B:HOH154 4.3 33.4 1.0 CA B:HIS77 4.5 19.6 1.0 O B:HOH198 4.5 32.8 1.0 O B:HOH147 4.6 46.2 1.0 CG1 B:VAL98 4.6 18.1 1.0 O B:HOH159 4.7 38.0 1.0 CG B:GLU99 4.7 42.3 1.0 CA B:GLU99 4.8 24.6 1.0 CB B:GLU102 4.9 19.6 1.0

A.M.Mcguire, B.J.Cuthbert, Z.Ma, K.D.Grauer-Gray, M.Brunjes Brophy, K.A.Spear, S.Soonsanga, J.I.Kliegman, S.L.Griner, J.D.Helmann, A.Glasfeld. Roles of the A and C Sites in the Manganese-Specific Activation of Mntr. Biochemistry V. 52 701 2013.
ISSN: ISSN 0006-2960
PubMed: 23298157
DOI: 10.1021/BI301550T