Manganese in PDB 6yxa: Structure of the Bifunctional Rel Enzyme From B. Subtilis

All present enzymatic activity of Structure of the Bifunctional Rel Enzyme From B. Subtilis:
2.7.6.5;

The structure of Structure of the Bifunctional Rel Enzyme From B. Subtilis, PDB code: 6yxa was solved by P.Pausch, G.Bange, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.72 / 3.95
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	130.152, 130.152, 157.621, 90.00, 90.00, 90.00
R / Rfree (%)	26.4 / 28.4

The binding sites of Manganese atom in the Structure of the Bifunctional Rel Enzyme From B. Subtilis (pdb code 6yxa). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Structure of the Bifunctional Rel Enzyme From B. Subtilis, PDB code: 6yxa:

Manganese binding site 1 out of 1 in the Structure of the Bifunctional Rel Enzyme From B. Subtilis


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of the Bifunctional Rel Enzyme From B. Subtilis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn601 b:0.5 occ:0.64 OD2 A:ASP144 2.2 0.5 1.0 OD1 A:ASP144 2.2 0.2 1.0 OD2 A:ASP78 2.2 0.7 1.0 NE2 A:HIS53 2.2 0.7 1.0 NE2 A:HIS77 2.2 0.8 1.0 CG A:ASP144 2.4 0.5 1.0 CD2 A:HIS77 2.9 0.9 1.0 CE1 A:HIS53 3.1 0.5 1.0 CG A:ASP78 3.2 0.0 1.0 CD2 A:HIS53 3.2 0.8 1.0 CE1 A:HIS77 3.4 0.1 1.0 OD1 A:ASP78 3.6 0.5 1.0 CB A:ASP144 3.8 0.8 1.0 CG A:HIS77 4.1 0.2 1.0 ND1 A:HIS53 4.3 0.7 1.0 CG A:HIS53 4.3 0.3 1.0 ND1 A:HIS77 4.3 0.6 1.0 CB A:ASP78 4.5 0.5 1.0 CA A:ASP144 4.6 0.7 1.0 ND2 A:ASN148 4.9 0.2 1.0

P.Pausch, M.Abdelshahid, W.Steinchen, H.Schafer, F.L.Gratani, S.A.Freibert, C.Wolz, K.Turgay, D.N.Wilson, G.Bange. Structural Basis For Regulation of the Opposing (P)Ppgpp Synthetase and Hydrolase Within the Stringent Response Orchestrator Rel. Cell Rep V. 32 08157 2020.
ISSN: ESSN 2211-1247
PubMed: 32937119
DOI: 10.1016/J.CELREP.2020.108157