Manganese in PDB 4irm: Crystal Structure of Mntc R116A Mutant Exhibits Flexibility in the C- Terminal Domain

The structure of Crystal Structure of Mntc R116A Mutant Exhibits Flexibility in the C- Terminal Domain, PDB code: 4irm was solved by M.Kanteev, N.Adir, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.50 / 3.50
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	128.400, 128.400, 90.510, 90.00, 90.00, 120.00
R / Rfree (%)	29.4 / 30.5

The binding sites of Manganese atom in the Crystal Structure of Mntc R116A Mutant Exhibits Flexibility in the C- Terminal Domain (pdb code 4irm). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the Crystal Structure of Mntc R116A Mutant Exhibits Flexibility in the C- Terminal Domain, PDB code: 4irm:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in the Crystal Structure of Mntc R116A Mutant Exhibits Flexibility in the C- Terminal Domain


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Mntc R116A Mutant Exhibits Flexibility in the C- Terminal Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:91.6 occ:1.00 OD1 A:ASP295 1.6 100.0 1.0 OE1 A:GLU220 1.7 0.5 1.0 NE2 A:HIS154 1.8 0.8 1.0 CD A:GLU220 2.1 95.3 1.0 OE2 A:GLU220 2.2 99.0 1.0 CE1 A:HIS154 2.3 99.9 1.0 CG A:ASP295 2.5 0.7 1.0 NE2 A:HIS89 2.6 0.7 1.0 CE1 A:HIS89 2.7 0.2 1.0 OD2 A:ASP295 2.8 0.3 1.0 CD2 A:HIS154 3.0 0.5 1.0 ND1 A:HIS154 3.5 94.2 1.0 CG A:GLU220 3.6 90.5 1.0 CB A:ASP295 3.9 0.3 1.0 CG A:HIS154 3.9 90.4 1.0 CD2 A:HIS89 3.9 96.9 1.0 ND1 A:HIS89 3.9 0.1 1.0 CD1 A:ILE240 4.0 97.6 1.0 OD1 A:ASN241 4.0 97.8 1.0 CA A:ASP295 4.3 93.3 1.0 CG A:ASN241 4.5 98.3 1.0 ND2 A:ASN241 4.5 96.6 1.0 CG A:HIS89 4.6 0.5 1.0 N A:ASP295 4.6 92.1 1.0 CB A:GLU220 4.6 97.8 1.0 CB A:ALA222 4.7 0.8 1.0 CG1 A:ILE240 5.0 96.0 1.0 CG1 A:ILE88 5.0 0.1 1.0

Manganese binding site 2 out of 3 in the Crystal Structure of Mntc R116A Mutant Exhibits Flexibility in the C- Terminal Domain


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Mntc R116A Mutant Exhibits Flexibility in the C- Terminal Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn401 b:0.9 occ:1.00 OE2 B:GLU220 1.8 0.6 1.0 OE1 B:GLU220 1.8 0.2 1.0 CD B:GLU220 1.9 1.0 1.0 OD2 B:ASP295 1.9 0.2 1.0 NE2 B:HIS154 2.0 0.8 1.0 CE1 B:HIS154 2.4 99.9 1.0 OD1 B:ASP295 2.4 0.6 1.0 CG B:ASP295 2.5 0.5 1.0 NE2 B:HIS89 2.5 0.4 1.0 CE1 B:HIS89 3.1 0.1 1.0 CG B:GLU220 3.3 0.2 1.0 CD2 B:HIS154 3.3 0.4 1.0 CD2 B:HIS89 3.6 0.9 1.0 ND1 B:HIS154 3.6 0.3 1.0 CB B:ASP295 4.0 0.7 1.0 CG B:HIS154 4.1 0.6 1.0 CB B:GLU220 4.2 0.8 1.0 ND1 B:HIS89 4.2 0.3 1.0 ND2 B:ASN241 4.3 0.9 1.0 CG B:HIS89 4.5 0.3 1.0 CB B:ALA222 4.7 0.4 1.0 CA B:ASP295 4.8 0.4 1.0 CG2 B:VAL294 4.9 0.3 1.0 OE1 B:GLU269 4.9 0.9 1.0 CG B:ASN241 4.9 0.2 1.0

Manganese binding site 3 out of 3 in the Crystal Structure of Mntc R116A Mutant Exhibits Flexibility in the C- Terminal Domain


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of Mntc R116A Mutant Exhibits Flexibility in the C- Terminal Domain within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn900 b:0.4 occ:1.00 CE1 C:HIS89 2.0 0.9 1.0 NE2 C:HIS154 2.2 0.2 1.0 CE1 C:HIS154 2.3 0.5 1.0 OD2 C:ASP295 2.4 0.6 1.0 OE1 C:GLU220 2.6 0.8 1.0 NE2 C:HIS89 2.6 0.3 1.0 OE2 C:GLU220 2.7 0.7 1.0 CD C:GLU220 2.7 0.0 1.0 ND2 C:ASN241 2.8 0.8 1.0 OD1 C:ASP295 2.8 0.1 1.0 CG C:ASP295 2.9 0.5 1.0 ND1 C:HIS89 3.2 0.4 1.0 CD2 C:HIS154 3.5 0.5 1.0 ND1 C:HIS154 3.7 0.1 1.0 CG C:ASN241 3.7 0.1 1.0 CG C:GLU220 3.8 0.6 1.0 CD2 C:HIS89 3.8 0.7 1.0 CG C:HIS89 4.1 0.5 1.0 CB C:ASN241 4.2 0.5 1.0 CG C:HIS154 4.2 0.6 1.0 CB C:ASP295 4.4 0.4 1.0 OD1 C:ASN241 4.5 0.6 1.0 CB C:GLU220 4.9 0.9 1.0 CB C:ALA222 5.0 0.3 1.0

M.Kanteev, N.Adir. Arginine 116 Stabilizes the Entrance to the Metal Ion-Binding Site of the Mntc Protein. Acta Crystallogr.,Sect.F V. 69 237 2013.
ISSN: ESSN 1744-3091
PubMed: 23519795
DOI: 10.1107/S174430911300153X