Iron in PDB 3r60: Structure of the Mntr FE2+ Complex

The structure of Structure of the Mntr FE2+ Complex, PDB code: 3r60 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)	21.82 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.680, 45.900, 74.690, 90.00, 93.50, 90.00
R / Rfree (%)	23.9 / 28.5

The binding sites of Iron atom in the Structure of the Mntr FE2+ Complex (pdb code 3r60). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of the Mntr FE2+ Complex, PDB code: 3r60:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of the Mntr FE2+ Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of the Mntr FE2+ Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe143 b:16.0 occ:1.00 O A:HOH144 2.2 22.7 1.0 OE2 A:GLU11 2.2 20.4 1.0 ND1 A:HIS77 2.2 16.1 1.0 OE2 A:GLU102 2.3 16.7 1.0 OE1 A:GLU102 2.3 17.9 1.0 CD A:GLU102 2.6 14.3 1.0 OE1 A:GLU11 2.8 22.2 1.0 CD A:GLU11 2.8 25.5 1.0 CE1 A:HIS77 3.2 10.2 1.0 CG A:HIS77 3.2 10.3 1.0 CB A:HIS77 3.6 10.9 1.0 OE1 A:GLU99 3.8 42.4 1.0 CD A:GLU99 4.0 31.5 1.0 CG A:GLU102 4.1 8.0 1.0 O A:HOH153 4.2 16.5 1.0 OE2 A:GLU99 4.2 35.3 1.0 O A:HOH164 4.3 19.8 1.0 NE2 A:HIS77 4.3 12.1 1.0 CG A:GLU11 4.3 20.3 1.0 CD2 A:HIS77 4.4 7.8 1.0 O A:HOH172 4.4 25.9 1.0 O A:HOH155 4.4 30.1 1.0 CA A:HIS77 4.5 7.4 1.0 O A:HOH165 4.6 36.7 1.0 CG A:GLU99 4.6 14.6 1.0 NE2 A:HIS103 4.8 24.3 1.0 CG1 A:VAL98 4.8 12.2 1.0 CE1 A:HIS103 4.9 21.4 1.0 CB A:GLU102 4.9 11.1 1.0 CA A:GLU99 5.0 10.3 1.0

Iron binding site 2 out of 2 in the Structure of the Mntr FE2+ Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of the Mntr FE2+ Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe143 b:17.9 occ:1.00 ND1 B:HIS77 2.1 14.5 1.0 O B:HOH144 2.1 23.2 1.0 OE2 B:GLU11 2.3 22.5 1.0 OE1 B:GLU102 2.3 15.2 1.0 OE2 B:GLU102 2.3 22.4 1.0 OE2 B:GLU99 2.4 35.8 1.0 CD B:GLU102 2.6 13.9 1.0 OE1 B:GLU11 2.8 25.3 1.0 CD B:GLU11 2.9 25.9 1.0 CE1 B:HIS77 3.0 16.4 1.0 CG B:HIS77 3.2 13.6 1.0 CB B:HIS77 3.6 12.2 1.0 CD B:GLU99 3.7 34.2 1.0 O B:HOH148 4.1 15.9 1.0 CG B:GLU102 4.1 13.3 1.0 NE2 B:HIS77 4.1 10.8 1.0 CD2 B:HIS77 4.2 8.7 1.0 O B:HOH169 4.3 30.5 1.0 O B:HOH203 4.3 22.4 1.0 OE1 B:GLU99 4.3 36.8 1.0 CG B:GLU11 4.4 17.9 1.0 O B:HOH146 4.5 25.3 1.0 CA B:HIS77 4.6 7.8 1.0 O B:HOH190 4.6 34.9 1.0 CG B:GLU99 4.7 16.2 1.0 CG1 B:VAL98 4.7 10.4 1.0 CB B:GLU102 4.9 12.2 1.0 NE2 B:HIS103 4.9 23.7 1.0 CE1 B:HIS103 4.9 23.3 1.0 CA B:GLU99 5.0 11.4 1.0 CE B:MET15 5.0 37.0 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