Cadmium in PDB 4hx7: Structure of Mntr E11K Mutant Complexed with CD2+

The structure of Structure of Mntr E11K Mutant Complexed with CD2+, PDB code: 4hx7 was solved by A.Glasfeld, B.J.Cuthbert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	74.00 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.119, 46.252, 74.142, 90.00, 92.99, 90.00
R / Rfree (%)	24.4 / 28.6

The binding sites of Cadmium atom in the Structure of Mntr E11K Mutant Complexed with CD2+ (pdb code 4hx7). This binding sites where shown within 5.0 Angstroms radius around Cadmium atom.
In total 2 binding sites of Cadmium where determined in the Structure of Mntr E11K Mutant Complexed with CD2+, PDB code: 4hx7:
Jump to Cadmium binding site number: 1; 2;

Cadmium binding site 1 out of 2 in the Structure of Mntr E11K Mutant Complexed with CD2+


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 1 of Structure of Mntr E11K Mutant Complexed with CD2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd201 b:20.4 occ:1.00 OE2 A:GLU102 2.3 21.1 1.0 O A:HOH315 2.3 28.4 1.0 NE2 A:HIS103 2.3 20.3 1.0 OD2 A:ASP8 2.4 14.3 1.0 O A:GLU99 2.5 13.6 1.0 OE1 A:GLU99 2.5 19.2 1.0 OD1 A:ASP8 3.1 24.4 1.0 CG A:ASP8 3.1 18.0 1.0 CD2 A:HIS103 3.3 17.2 1.0 CE1 A:HIS103 3.3 18.2 1.0 C A:GLU99 3.3 17.6 1.0 CD A:GLU102 3.4 24.4 1.0 CD A:GLU99 3.5 20.9 1.0 CA A:GLU99 3.5 18.5 1.0 CG A:GLU102 3.8 22.3 1.0 CB A:GLU99 3.8 18.1 1.0 CG A:GLU99 4.3 17.9 1.0 OE2 A:GLU99 4.3 19.5 1.0 ND1 A:HIS103 4.4 16.7 1.0 CG A:HIS103 4.4 20.2 1.0 O A:HOH324 4.4 33.6 1.0 NZ A:LYS11 4.4 20.2 1.0 OE1 A:GLU102 4.5 28.7 1.0 CB A:ASP8 4.6 14.0 1.0 N A:GLY100 4.6 13.1 1.0 N A:GLU99 4.9 14.9 1.0

Cadmium binding site 2 out of 2 in the Structure of Mntr E11K Mutant Complexed with CD2+


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 2 of Structure of Mntr E11K Mutant Complexed with CD2+ within 5.0Å range: probe atom residue distance (Å) B Occ B:Cd201 b:19.9 occ:1.00 OE1 B:GLU99 2.3 22.7 1.0 OE2 B:GLU102 2.3 19.6 1.0 NE2 B:HIS103 2.4 24.3 1.0 O B:GLU99 2.4 16.9 1.0 O B:HOH330 2.4 18.4 1.0 OD2 B:ASP8 2.5 24.5 1.0 CE1 B:HIS103 3.2 22.2 1.0 C B:GLU99 3.3 16.3 1.0 CG B:ASP8 3.4 21.6 1.0 CD2 B:HIS103 3.4 23.4 1.0 CD B:GLU102 3.4 21.0 1.0 CD B:GLU99 3.4 24.2 1.0 CA B:GLU99 3.6 14.8 1.0 OD1 B:ASP8 3.6 24.4 1.0 CG B:GLU102 3.8 14.8 1.0 CB B:GLU99 3.8 18.8 1.0 CG B:GLU99 4.2 19.9 1.0 OE2 B:GLU99 4.2 21.4 1.0 ND1 B:HIS103 4.3 20.6 1.0 CG B:HIS103 4.4 24.4 1.0 NZ B:LYS11 4.5 15.5 1.0 OE1 B:GLU102 4.5 24.8 1.0 N B:GLY100 4.5 17.0 1.0 CB B:ASP8 4.8 20.9 1.0 N B:GLU99 4.9 14.8 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