Manganese in PDB 8e6h: X-Ray Structure of the Deinococcus Radiodurans Nramp/Mnth Divalent Transition Metal Transporter A47W Mutant in An Occluded, Manganese- Bound State

The structure of X-Ray Structure of the Deinococcus Radiodurans Nramp/Mnth Divalent Transition Metal Transporter A47W Mutant in An Occluded, Manganese- Bound State, PDB code: 8e6h was solved by S.Ray, R.Gaudet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.35 / 2.39
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.98, 70.929, 98.571, 90, 90, 90
R / Rfree (%)	20.6 / 24.6

The structure of X-Ray Structure of the Deinococcus Radiodurans Nramp/Mnth Divalent Transition Metal Transporter A47W Mutant in An Occluded, Manganese- Bound State also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Manganese atom in the X-Ray Structure of the Deinococcus Radiodurans Nramp/Mnth Divalent Transition Metal Transporter A47W Mutant in An Occluded, Manganese- Bound State (pdb code 8e6h). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the X-Ray Structure of the Deinococcus Radiodurans Nramp/Mnth Divalent Transition Metal Transporter A47W Mutant in An Occluded, Manganese- Bound State, PDB code: 8e6h:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the X-Ray Structure of the Deinococcus Radiodurans Nramp/Mnth Divalent Transition Metal Transporter A47W Mutant in An Occluded, Manganese- Bound State


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of X-Ray Structure of the Deinococcus Radiodurans Nramp/Mnth Divalent Transition Metal Transporter A47W Mutant in An Occluded, Manganese- Bound State within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn501 b:39.5 occ:0.71 O A:ALA53 2.1 49.1 1.0 O A:HOH604 2.2 56.3 1.0 O A:ALA227 2.2 36.9 1.0 OD1 A:ASN59 2.5 32.5 1.0 OD1 A:ASP56 2.6 52.6 1.0 SD A:MET230 2.8 56.1 1.0 C A:ALA53 3.3 61.3 1.0 C A:ALA227 3.4 34.4 1.0 CE A:MET230 3.4 44.5 1.0 CG A:ASP56 3.4 46.7 1.0 CG A:ASN59 3.5 35.6 1.0 CG A:MET230 3.8 42.4 1.0 CA A:ALA227 3.9 29.9 1.0 ND2 A:ASN59 4.0 40.0 1.0 OD2 A:ASP56 4.0 56.7 1.0 CA A:TYR54 4.0 45.2 1.0 N A:TYR54 4.0 59.9 1.0 C A:TYR54 4.3 43.1 1.0 CA A:ALA53 4.4 50.0 1.0 CB A:ASP56 4.4 42.1 1.0 CB A:ALA227 4.4 31.3 1.0 N A:THR228 4.5 28.3 1.0 N A:ASP56 4.5 40.0 1.0 N A:MET55 4.7 59.1 1.0 CB A:ASN59 4.7 30.4 1.0 N A:ASN59 4.7 29.1 1.0 OE1 A:GLN378 4.7 36.0 1.0 CB A:ALA53 4.7 44.6 1.0 O A:TYR54 4.8 51.4 1.0 CA A:THR228 4.8 31.0 1.0

Manganese binding site 2 out of 2 in the X-Ray Structure of the Deinococcus Radiodurans Nramp/Mnth Divalent Transition Metal Transporter A47W Mutant in An Occluded, Manganese- Bound State


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of X-Ray Structure of the Deinococcus Radiodurans Nramp/Mnth Divalent Transition Metal Transporter A47W Mutant in An Occluded, Manganese- Bound State within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn502 b:42.3 occ:1.00 OD1 A:ASP369 2.1 45.3 1.0 O A:HOH657 2.1 52.7 1.0 OD1 A:ASP296 2.2 49.3 1.0 OD2 A:ASP296 2.5 44.2 1.0 O A:HOH637 2.5 31.3 1.0 CG A:ASP296 2.6 49.4 1.0 CG A:ASP369 3.1 45.0 1.0 O A:HOH621 3.1 65.7 1.0 O A:HOH674 3.2 55.6 1.0 OD2 A:ASP369 3.4 47.4 1.0 CB A:ASP296 4.1 49.5 1.0 O A:HOH667 4.1 55.5 1.0 CG2 A:THR298 4.2 42.6 1.0 OG A:SER371 4.2 42.6 1.0 CD A:PRO370 4.3 40.8 1.0 OG1 A:THR298 4.3 46.2 1.0 O A:HOH639 4.4 47.4 1.0 CB A:ASP369 4.4 36.5 1.0 CB A:SER371 4.6 39.0 1.0 O A:HOH650 4.6 44.3 1.0 N A:SER371 4.7 37.7 1.0 OD1 A:ASN293 4.7 104.7 1.0 N A:PRO370 4.8 37.6 1.0 CA A:ASP369 4.9 41.2 1.0 CB A:THR298 4.9 37.4 1.0

S.Ray, S.P.Berry, E.A.Wilson, C.H.Zhang, M.Shekhar, A.Singharoy, R.Gaudet. High-Resolution Structures with Bound Mn 2+ and Cd 2+ Map the Metal Import Pathway in An Nramp Transporter. Elife V. 12 2023.
ISSN: ESSN 2050-084X
PubMed: 37039477
DOI: 10.7554/ELIFE.84006