Manganese in PDB 4y6u: Mycobacterial Protein

All present enzymatic activity of Mycobacterial Protein:
2.4.1.266;

The structure of Mycobacterial Protein, PDB code: 4y6u was solved by D.Albesa-Jove, A.Rodrigo-Unzueta, J.O.Cifuente, S.Urresti, N.Comino, E.Sancho-Vaello, M.E.Guerin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	70.20 / 2.27
Space group	I 41
Cell size a, b, c (Å), α, β, γ (°)	99.280, 99.280, 128.230, 90.00, 90.00, 90.00
R / Rfree (%)	18.4 / 21.2

The structure of Mycobacterial Protein also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Manganese atom in the Mycobacterial Protein (pdb code 4y6u). 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 Mycobacterial Protein, PDB code: 4y6u:

Manganese binding site 1 out of 1 in the Mycobacterial Protein


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Mycobacterial Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:47.4 occ:1.00 O A:HOH516 2.2 49.9 1.0 O A:HOH531 2.2 45.5 1.0 O1A A:UPG404 2.3 50.4 1.0 OD2 A:ASP136 2.3 42.9 1.0 ND1 A:HIS258 2.3 51.2 1.0 O2B A:UPG404 2.4 49.3 1.0 CE1 A:HIS258 3.1 47.2 1.0 CG A:ASP136 3.2 41.8 1.0 CG A:HIS258 3.4 52.9 1.0 PB A:UPG404 3.4 47.9 1.0 OD1 A:ASP136 3.5 39.9 1.0 PA A:UPG404 3.5 44.3 1.0 O3A A:UPG404 3.7 52.6 1.0 CB A:HIS258 3.8 49.2 1.0 O2' A:UPG404 3.9 49.3 1.0 O1B A:UPG404 4.0 49.5 1.0 NH1 A:ARG259 4.1 48.8 0.5 O A:ARG259 4.1 61.1 1.0 NE2 A:HIS258 4.3 51.8 1.0 N A:ARG259 4.3 51.7 1.0 NH2 A:ARG259 4.3 39.0 0.5 CZ A:ARG259 4.4 46.8 0.5 CD2 A:HIS258 4.4 58.3 1.0 O5C A:UPG404 4.5 41.2 1.0 C5C A:UPG404 4.5 41.7 1.0 CB A:ASP136 4.5 42.0 1.0 O2A A:UPG404 4.5 37.0 1.0 NH2 A:ARG256 4.6 57.9 1.0 OD2 A:ASP134 4.7 45.7 1.0 O3B A:UPG404 4.7 46.7 1.0 CB A:ARG259 4.8 50.0 0.5 CB A:ARG259 4.8 50.0 0.5 CA A:ARG259 4.9 50.2 0.5 CA A:ARG259 4.9 50.2 0.5 C A:ARG259 4.9 55.3 1.0 C A:HIS258 5.0 48.6 1.0 CA A:HIS258 5.0 45.7 1.0

D.Albesa-Jove, F.Mendoza, A.Rodrigo-Unzueta, F.Gomollon-Bel, J.O.Cifuente, S.Urresti, N.Comino, H.Gomez, J.Romero-Garcia, J.M.Lluch, E.Sancho-Vaello, X.Biarnes, A.Planas, P.Merino, L.Masgrau, M.E.Guerin. A Native Ternary Complex Trapped in A Crystal Reveals the Catalytic Mechanism of A Retaining Glycosyltransferase. Angew.Chem.Int.Ed.Engl. V. 54 9898 2015.
ISSN: ESSN 1521-3773
PubMed: 26136334
DOI: 10.1002/ANIE.201504617