Manganese in PDB 6x5r: Human Alpha-1,6-Fucosyltransferase (FUT8) Bound to Gdp and A2-Asn

All present enzymatic activity of Human Alpha-1,6-Fucosyltransferase (FUT8) Bound to Gdp and A2-Asn:
2.4.1.68;

The structure of Human Alpha-1,6-Fucosyltransferase (FUT8) Bound to Gdp and A2-Asn, PDB code: 6x5r was solved by R.Kadirvelraj, Z.A.Wood, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.41 / 2.40
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	149.880, 149.880, 480.880, 90.00, 90.00, 120.00
R / Rfree (%)	20.5 / 23.1

The binding sites of Manganese atom in the Human Alpha-1,6-Fucosyltransferase (FUT8) Bound to Gdp and A2-Asn (pdb code 6x5r). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Human Alpha-1,6-Fucosyltransferase (FUT8) Bound to Gdp and A2-Asn, PDB code: 6x5r:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Human Alpha-1,6-Fucosyltransferase (FUT8) Bound to Gdp and A2-Asn


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Human Alpha-1,6-Fucosyltransferase (FUT8) Bound to Gdp and A2-Asn within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn800 b:71.1 occ:0.80 NE2 A:HIS491 2.2 78.2 1.0 O A:HOH856 2.5 60.8 1.0 NE2 A:HIS389 2.6 69.7 1.0 CD2 A:HIS491 3.1 78.6 1.0 O A:HOH1039 3.1 50.1 1.0 CE1 A:HIS491 3.3 81.2 1.0 CD2 A:HIS389 3.4 67.4 1.0 CE1 A:HIS389 3.6 67.2 1.0 OE1 A:GLU388 3.7 80.0 1.0 ND1 A:HIS385 4.2 52.4 1.0 CG A:HIS491 4.3 73.2 1.0 ND1 A:HIS491 4.4 79.0 1.0 CG A:HIS389 4.5 68.1 1.0 ND1 A:HIS389 4.6 71.5 1.0 CE1 A:HIS385 4.9 49.5 1.0 CD A:GLU388 4.9 73.6 1.0 CB A:GLU388 5.0 51.4 1.0

Manganese binding site 2 out of 2 in the Human Alpha-1,6-Fucosyltransferase (FUT8) Bound to Gdp and A2-Asn


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Human Alpha-1,6-Fucosyltransferase (FUT8) Bound to Gdp and A2-Asn within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn800 b:85.0 occ:0.80 NE2 B:HIS491 2.4 70.3 1.0 NE2 B:HIS389 2.5 68.4 1.0 O B:HOH836 2.5 63.7 1.0 CD2 B:HIS491 3.1 69.0 1.0 CD2 B:HIS389 3.2 67.6 1.0 CE1 B:HIS491 3.5 72.3 1.0 CE1 B:HIS389 3.6 68.8 1.0 OE1 B:GLU388 3.6 84.6 1.0 O B:HOH1017 4.1 73.2 1.0 ND1 B:HIS385 4.3 46.3 1.0 CG B:HIS491 4.4 61.1 1.0 CG B:HIS389 4.4 71.2 1.0 ND1 B:HIS491 4.5 65.6 1.0 ND1 B:HIS389 4.6 70.7 1.0 CD B:GLU388 4.9 74.7 1.0 CB B:GLU388 4.9 46.3 1.0 CZ B:PHE462 5.0 38.7 1.0

B.M.Boruah, R.Kadirvelraj, L.Liu, A.Ramiah, C.Li, G.Zong, G.P.Bosman, J.Y.Yang, L.X.Wang, G.J.Boons, Z.A.Wood, K.W.Moremen. Characterizing Human Alpha-1,6-Fucosyltransferase (FUT8) Substrate Specificity and Structural Similarities with Related Fucosyltransferases. J.Biol.Chem. 2020.
ISSN: ESSN 1083-351X
PubMed: 33004438
DOI: 10.1074/JBC.RA120.014625