Manganese in PDB 5kss: Stationary Phase Survival Protein E (Sure) From Xylella Fastidiosa - Xfsure-Ds (Dimer Smaller)

All present enzymatic activity of Stationary Phase Survival Protein E (Sure) From Xylella Fastidiosa - Xfsure-Ds (Dimer Smaller):
3.1.3.5;

The structure of Stationary Phase Survival Protein E (Sure) From Xylella Fastidiosa - Xfsure-Ds (Dimer Smaller), PDB code: 5kss was solved by A.T.P.Machado, E.M.B.Fonseca, M.A.Dos Reis, A.M.Saraiva, C.A.Dos Santos, A.M.S.De Toledo, I.Polikarpov, A.P.De Souza, R.Aparicio, J.Iulek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.94 / 2.82
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	86.941, 80.118, 71.511, 90.00, 95.51, 90.00
R / Rfree (%)	27.2 / 32.9

The structure of Stationary Phase Survival Protein E (Sure) From Xylella Fastidiosa - Xfsure-Ds (Dimer Smaller) also contains other interesting chemical elements:

Iodine	(I)	3 atoms
Chlorine	(Cl)	2 atoms

The binding sites of Manganese atom in the Stationary Phase Survival Protein E (Sure) From Xylella Fastidiosa - Xfsure-Ds (Dimer Smaller) (pdb code 5kss). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Stationary Phase Survival Protein E (Sure) From Xylella Fastidiosa - Xfsure-Ds (Dimer Smaller), PDB code: 5kss:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Stationary Phase Survival Protein E (Sure) From Xylella Fastidiosa - Xfsure-Ds (Dimer Smaller)


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Stationary Phase Survival Protein E (Sure) From Xylella Fastidiosa - Xfsure-Ds (Dimer Smaller) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn501 b:57.8 occ:1.00 OD1 A:ASN92 2.1 53.7 1.0 OD1 A:ASP9 2.2 48.9 1.0 OG A:SER40 2.9 86.0 1.0 CG A:ASN92 3.1 56.5 1.0 CB A:ASP8 3.2 69.2 1.0 CL A:CL504 3.2 60.4 1.0 CG A:ASP8 3.3 70.7 1.0 OD1 A:ASN93 3.3 60.5 1.0 OD2 A:ASP8 3.4 71.0 1.0 CG A:ASP9 3.4 63.7 1.0 ND2 A:ASN92 3.5 60.6 1.0 N A:ASP9 3.9 69.2 1.0 OD1 A:ASP8 4.0 74.3 1.0 C A:ASP8 4.0 69.2 1.0 OD1 A:ASP38 4.2 86.8 1.0 CB A:SER40 4.2 86.0 1.0 OD2 A:ASP9 4.2 62.1 1.0 CA A:ASP8 4.2 68.3 1.0 OG1 A:THR106 4.3 43.7 1.0 CA A:ASP9 4.3 68.0 1.0 CG A:ASN93 4.3 62.1 1.0 CB A:ASN92 4.4 56.6 1.0 CB A:ASP9 4.4 67.1 1.0 O A:ASP8 4.6 70.8 1.0 N A:ASN93 4.7 62.4 1.0 CA A:ASN92 4.9 58.4 1.0 N A:ASP8 4.9 68.2 1.0 OD2 A:ASP38 4.9 87.1 1.0 CG A:ASP38 5.0 87.5 1.0 ND2 A:ASN93 5.0 62.3 1.0

Manganese binding site 2 out of 2 in the Stationary Phase Survival Protein E (Sure) From Xylella Fastidiosa - Xfsure-Ds (Dimer Smaller)


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Stationary Phase Survival Protein E (Sure) From Xylella Fastidiosa - Xfsure-Ds (Dimer Smaller) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn501 b:66.5 occ:1.00 OD1 B:ASN92 2.1 70.0 1.0 OD1 B:ASP9 2.2 65.0 1.0 OG B:SER40 2.9 82.0 1.0 CG B:ASN92 3.1 69.8 1.0 OD1 B:ASN93 3.2 74.0 1.0 CB B:ASP8 3.3 64.7 1.0 ND2 B:ASN92 3.4 68.7 1.0 CG B:ASP8 3.4 68.7 1.0 CG B:ASP9 3.5 67.2 1.0 OD2 B:ASP8 3.5 68.7 1.0 CL B:CL502 3.7 77.9 1.0 N B:ASP9 4.0 61.0 1.0 OD1 B:ASP8 4.1 74.1 1.0 CB B:SER40 4.2 82.7 1.0 C B:ASP8 4.2 61.1 1.0 OD2 B:ASP9 4.2 70.6 1.0 CG B:ASN93 4.2 72.5 1.0 OD1 B:ASP38 4.3 85.3 1.0 OG1 B:THR106 4.4 69.8 1.0 CA B:ASP8 4.4 62.5 1.0 CA B:ASP9 4.4 63.1 1.0 CB B:ASN92 4.4 70.9 1.0 CB B:ASP9 4.5 65.2 1.0 N B:ASN93 4.6 71.5 1.0 O B:ASP8 4.7 60.3 1.0 ND2 B:ASN93 4.8 71.5 1.0 CA B:ASN92 4.9 70.6 1.0 OG1 B:THR94 4.9 57.8 1.0 OD2 B:ASP38 5.0 87.9 1.0

A.T.P.Machado, E.M.B.Fonseca, M.A.D.Reis, A.M.Saraiva, C.A.D.Santos, M.A.S.De Toledo, I.Polikarpov, A.P.De Souza, R.Aparicio, J.Iulek. Conformational Variability of the Stationary Phase Survival Protein E From Xylella Fastidiosa Revealed By X-Ray Crystallography, Small-Angle X-Ray Scattering Studies, and Normal Mode Analysis. Proteins V. 85 1931 2017.
ISSN: ESSN 1097-0134
PubMed: 28677327
DOI: 10.1002/PROT.25347