Manganese in PDB 4y63: Aaglyb in Complex with Amino-Acid Analogues

All present enzymatic activity of Aaglyb in Complex with Amino-Acid Analogues:
2.4.1.37; 2.4.1.40;

The structure of Aaglyb in Complex with Amino-Acid Analogues, PDB code: 4y63 was solved by S.Wang, J.A.Cuesta-Seijo, A.Striebeck, D.Lafont, M.M.Palcic, S.Vidal, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.30 / 1.30
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	52.840, 149.150, 80.090, 90.00, 90.00, 90.00
R / Rfree (%)	15.9 / 18.3

The binding sites of Manganese atom in the Aaglyb in Complex with Amino-Acid Analogues (pdb code 4y63). 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 Aaglyb in Complex with Amino-Acid Analogues, PDB code: 4y63:

Manganese binding site 1 out of 1 in the Aaglyb in Complex with Amino-Acid Analogues


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Aaglyb in Complex with Amino-Acid Analogues within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn403 b:16.6 occ:0.40 O6 A:48O402 2.0 23.2 1.0 O A:HOH508 2.1 26.0 1.0 O A:HOH708 2.2 34.1 1.0 O A:HOH537 2.3 24.9 1.0 OD2 A:ASP213 2.3 15.6 1.0 C12 A:48O402 2.8 30.1 1.0 C10 A:48O402 2.9 24.1 1.0 CG A:ASP213 3.1 13.1 1.0 OD1 A:ASP213 3.2 15.0 1.0 C11 A:48O402 3.3 28.0 1.0 O A:HOH637 3.8 22.5 1.0 OD2 A:ASP211 4.0 13.9 1.0 O2 A:BHE401 4.1 17.9 1.0 N4 A:48O402 4.2 19.6 1.0 O A:HOH638 4.2 28.2 1.0 O A:HOH729 4.4 30.3 1.0 O A:HOH569 4.4 29.3 1.0 O A:HOH658 4.4 32.2 1.0 O5 A:48O402 4.5 14.0 1.0 C2 A:BHE401 4.5 17.9 1.0 CB A:ASP213 4.6 12.1 1.0 N1 A:48O402 4.7 31.1 1.0 C9 A:48O402 4.7 19.6 1.0 CE2 A:TYR126 4.8 16.7 1.0 OH A:TYR126 4.8 20.3 1.0 C7 A:48O402 4.9 16.1 1.0 CG A:ASP211 4.9 11.3 1.0

S.Wang, J.A.Cuesta-Seijo, A.Striebeck, D.Lafont, M.M.Palcic, S.Vidal. Design of Glycosyltransferase Inhibitors: Serine Analogues As Pyrophosphate Surrogates? Chempluschem V. 80 1525 2015.
ISSN: ESSN 2192-6506
DOI: 10.1002/CPLU.201500282