Manganese in PDB 1o7o: Roles of Individual Residues of Alpha-1,3 Galactosyltransferases in Substrate Binding and Catalysis

All present enzymatic activity of Roles of Individual Residues of Alpha-1,3 Galactosyltransferases in Substrate Binding and Catalysis:
2.4.1.151;

The structure of Roles of Individual Residues of Alpha-1,3 Galactosyltransferases in Substrate Binding and Catalysis, PDB code: 1o7o was solved by Y.Zhang, G.J.Swaminathan, A.Deshpande, R.Natesh, Z.Xie, K.R.Acharya, K.Brew, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.97
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	45.202, 94.288, 94.675, 90.00, 99.10, 90.00
R / Rfree (%)	18.1 / 20.6

The binding sites of Manganese atom in the Roles of Individual Residues of Alpha-1,3 Galactosyltransferases in Substrate Binding and Catalysis (pdb code 1o7o). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Roles of Individual Residues of Alpha-1,3 Galactosyltransferases in Substrate Binding and Catalysis, PDB code: 1o7o:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Roles of Individual Residues of Alpha-1,3 Galactosyltransferases in Substrate Binding and Catalysis


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Roles of Individual Residues of Alpha-1,3 Galactosyltransferases in Substrate Binding and Catalysis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1001 b:12.9 occ:1.00 O1B A:UDP1371 2.2 11.2 1.0 OD1 A:ASP227 2.3 13.3 1.0 OD2 A:ASP225 2.3 8.9 1.0 O A:HOH2286 2.3 15.7 1.0 O1A A:UDP1371 2.3 12.4 1.0 OD2 A:ASP227 2.5 12.9 1.0 CG A:ASP227 2.7 11.6 1.0 CG A:ASP225 3.2 9.3 1.0 PB A:UDP1371 3.4 14.5 1.0 PA A:UDP1371 3.4 13.4 1.0 O3A A:UDP1371 3.4 14.5 1.0 CB A:ASP225 3.5 9.8 1.0 NZ A:LYS359 3.7 8.0 1.0 O3' A:UDP1371 3.7 12.4 1.0 O3B A:UDP1371 3.8 15.0 1.0 O A:HOH2209 4.1 32.8 1.0 O A:HOH2275 4.2 19.3 1.0 CB A:ASP227 4.2 10.3 1.0 O5' A:UDP1371 4.2 13.2 1.0 OD1 A:ASP225 4.3 10.0 1.0 C5' A:UDP1371 4.4 10.4 1.0 O A:HOH2291 4.4 12.4 1.0 C3' A:UDP1371 4.5 9.9 1.0 O A:HOH2155 4.6 16.9 1.0 O2B A:UDP1371 4.6 15.7 1.0 O2A A:UDP1371 4.6 13.2 1.0 O A:HOH2273 4.6 9.6 1.0 O A:HOH2154 4.7 22.8 1.0 CB A:ALA282 4.8 9.0 1.0 C4' A:UDP1371 4.8 10.3 1.0 O A:ASP227 4.8 12.6 1.0 N A:ASP227 4.9 9.6 1.0 CA A:ASP225 5.0 8.7 1.0 CA A:ASP227 5.0 10.5 1.0

Manganese binding site 2 out of 2 in the Roles of Individual Residues of Alpha-1,3 Galactosyltransferases in Substrate Binding and Catalysis


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Roles of Individual Residues of Alpha-1,3 Galactosyltransferases in Substrate Binding and Catalysis within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn1002 b:12.9 occ:1.00 O1B B:UDP2371 2.2 10.2 1.0 OD2 B:ASP1225 2.2 8.7 1.0 OD1 B:ASP1227 2.2 12.5 1.0 O B:HOH2002 2.3 13.3 1.0 O1A B:UDP2371 2.3 10.1 1.0 OD2 B:ASP1227 2.5 10.9 1.0 CG B:ASP1227 2.7 11.8 1.0 CG B:ASP1225 3.2 9.7 1.0 PB B:UDP2371 3.3 12.4 1.0 PA B:UDP2371 3.4 10.6 1.0 O3A B:UDP2371 3.4 10.5 1.0 CB B:ASP1225 3.5 7.7 1.0 NZ B:LYS1359 3.7 7.6 1.0 O3B B:UDP2371 3.7 11.3 1.0 O3' B:UDP2371 3.8 9.5 1.0 O B:HOH2302 4.0 25.8 1.0 O B:HOH2297 4.1 18.9 1.0 CB B:ASP1227 4.2 11.0 1.0 O5' B:UDP2371 4.3 11.2 1.0 OD1 B:ASP1225 4.3 10.4 1.0 C5' B:UDP2371 4.4 9.2 1.0 O B:HOH2146 4.4 13.1 1.0 O B:HOH2141 4.6 24.2 1.0 O2B B:UDP2371 4.6 13.7 1.0 C3' B:UDP2371 4.6 8.4 1.0 O B:HOH2147 4.6 13.0 1.0 O2A B:UDP2371 4.6 12.2 1.0 O B:HOH2281 4.7 10.3 1.0 CB B:ALA1282 4.7 8.8 1.0 O B:ASP1227 4.9 10.1 1.0 C4' B:UDP2371 4.9 8.6 1.0 CA B:ASP1225 4.9 8.7 1.0 N B:ASP1227 5.0 9.4 1.0

Y.Zhang, G.J.Swaminathan, A.Deshpande, E.Boix, R.Natesh, Z.Xie, K.R.Acharya, K.Brew. Roles of Individual Enzyme-Substrate Interactions By Alpha-1,3-Galactosyltransferase in Catalysis and Specificity. Biochemistry V. 42 13512 2003.
ISSN: ISSN 0006-2960
PubMed: 14621997
DOI: 10.1021/BI035430R