Manganese in PDB 5uyf: Yfea From M9 Minimal Media Supplemented with Zinc - Mn Wavelength

The structure of Yfea From M9 Minimal Media Supplemented with Zinc - Mn Wavelength, PDB code: 5uyf was solved by C.D.Radka, L.J.Delucas, S.G.Aller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.30 / 2.06
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	41.859, 52.191, 112.762, 90.00, 90.00, 90.00
R / Rfree (%)	16.2 / 20

The binding sites of Manganese atom in the Yfea From M9 Minimal Media Supplemented with Zinc - Mn Wavelength (pdb code 5uyf). 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 Yfea From M9 Minimal Media Supplemented with Zinc - Mn Wavelength, PDB code: 5uyf:

Manganese binding site 1 out of 1 in the Yfea From M9 Minimal Media Supplemented with Zinc - Mn Wavelength


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Yfea From M9 Minimal Media Supplemented with Zinc - Mn Wavelength within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:20.2 occ:1.00 NE2 A:HIS76 2.0 25.3 1.0 OE1 A:GLU207 2.0 23.2 1.0 NE2 A:HIS141 2.1 23.2 1.0 OD2 A:ASP282 2.1 29.4 1.0 OD1 A:ASP282 2.5 27.4 1.0 CG A:ASP282 2.7 27.6 1.0 CD A:GLU207 2.7 27.3 1.0 OE2 A:GLU207 2.7 27.9 1.0 CE1 A:HIS76 2.9 26.8 1.0 CE1 A:HIS141 3.0 24.2 1.0 CD2 A:HIS76 3.0 25.6 1.0 CD2 A:HIS141 3.2 24.3 1.0 ND2 A:ASN228 3.9 27.8 1.0 ND1 A:HIS76 4.0 24.2 1.0 CG A:HIS76 4.1 26.8 1.0 ND1 A:HIS141 4.2 21.7 1.0 CG A:GLU207 4.2 25.5 1.0 CB A:ASP282 4.2 26.4 1.0 O A:HOH571 4.2 32.7 1.0 CG A:HIS141 4.3 28.4 1.0 CG A:ASN228 4.3 29.9 1.0 CB A:ALA209 4.4 24.4 1.0 O A:HOH515 4.4 29.7 1.0 OD1 A:ASN228 4.6 31.0 1.0 CD1 A:LEU101 4.9 23.4 1.0 CB A:ASN228 4.9 29.8 1.0 CB A:GLU207 5.0 25.4 1.0

C.D.Radka, L.J.Delucas, L.S.Wilson, M.B.Lawrenz, R.D.Perry, S.G.Aller. Crystal Structure of Yersinia Pestis Virulence Factor Yfea Reveals Two Polyspecific Metal-Binding Sites. Acta Crystallogr D Struct V. 73 557 2017BIOL.
ISSN: ISSN 2059-7983
PubMed: 28695856
DOI: 10.1107/S2059798317006349