Manganese in PDB 4hv6: Structure of Mntr H77A Mutant in Apo- and Mn-Bound Forms

The structure of Structure of Mntr H77A Mutant in Apo- and Mn-Bound Forms, PDB code: 4hv6 was solved by A.Glasfeld, K.Grauer-Gray, A.Mcguire, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.80 / 2.30
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	51.734, 51.734, 175.564, 90.00, 90.00, 120.00
R / Rfree (%)	25.2 / 31.7

The structure of Structure of Mntr H77A Mutant in Apo- and Mn-Bound Forms also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Manganese atom in the Structure of Mntr H77A Mutant in Apo- and Mn-Bound Forms (pdb code 4hv6). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Structure of Mntr H77A Mutant in Apo- and Mn-Bound Forms, PDB code: 4hv6:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Structure of Mntr H77A Mutant in Apo- and Mn-Bound Forms


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of Mntr H77A Mutant in Apo- and Mn-Bound Forms within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn201 b:51.3 occ:1.00 OE1 A:GLU99 1.9 58.1 1.0 NE2 A:HIS103 2.2 52.3 1.0 O A:GLU99 2.3 35.7 1.0 OE2 A:GLU102 2.4 36.2 1.0 O A:HOH301 2.4 50.0 1.0 OD2 A:ASP8 2.7 59.2 1.0 OD1 A:ASP8 2.8 60.6 1.0 CD A:GLU99 3.0 64.5 1.0 CE1 A:HIS103 3.1 54.3 1.0 CG A:ASP8 3.1 53.4 1.0 CD2 A:HIS103 3.2 45.8 1.0 C A:GLU99 3.3 41.2 1.0 CD A:GLU102 3.4 39.1 1.0 CG A:GLU99 3.6 58.5 1.0 CA A:GLU99 3.7 39.8 1.0 CG A:GLU102 3.8 39.0 1.0 MN A:MN202 3.8 65.7 1.0 OE2 A:GLU99 4.1 73.0 1.0 ND1 A:HIS103 4.2 52.7 1.0 CB A:GLU99 4.2 44.9 1.0 CG A:HIS103 4.3 51.0 1.0 OE1 A:GLU102 4.5 42.5 1.0 N A:GLY100 4.5 43.6 1.0 CB A:ASP8 4.6 50.3 1.0 O A:VAL98 4.8 36.3 1.0 CA A:GLY100 4.9 41.9 1.0 N A:GLU99 5.0 40.9 1.0

Manganese binding site 2 out of 2 in the Structure of Mntr H77A Mutant in Apo- and Mn-Bound Forms


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of Mntr H77A Mutant in Apo- and Mn-Bound Forms within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn202 b:65.7 occ:1.00 OE2 A:GLU102 2.2 36.2 1.0 OE1 A:GLU11 2.3 58.5 1.0 O A:HOH306 2.4 56.5 1.0 OD2 A:ASP8 2.9 59.2 1.0 CD A:GLU102 2.9 39.1 1.0 OE1 A:GLU102 2.9 42.5 1.0 CD A:GLU11 3.0 56.0 1.0 OE2 A:GLU11 3.0 62.6 1.0 OE1 A:GLU99 3.3 58.1 1.0 O A:HOH302 3.4 60.4 1.0 MN A:MN201 3.8 51.3 1.0 OE2 A:GLU99 4.0 73.0 1.0 CD A:GLU99 4.0 64.5 1.0 CG A:ASP8 4.1 53.4 1.0 CG A:GLU102 4.4 39.0 1.0 CG A:GLU11 4.4 55.7 1.0 CA A:ASP8 4.8 46.9 1.0 CB A:GLU11 4.8 53.0 1.0 CB A:ALA77 4.8 35.7 1.0 CE1 A:HIS103 4.9 54.3 1.0 OD1 A:ASP8 4.9 60.6 1.0 CB A:ASP8 4.9 50.3 1.0 NE2 A:HIS103 4.9 52.3 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