Manganese in PDB 1vzt: 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: 1vzt was solved by Y.Zhang, G.J.Swaminathan, A.Deshpande, R.Natesh, X.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 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	45.058, 94.211, 94.570, 90.00, 98.96, 90.00
R / Rfree (%)	19.3 / 22

The binding sites of Manganese atom in the Roles of Individual Residues of Alpha-1,3 Galactosyltransferases in Substrate Binding and Catalysis (pdb code 1vzt). 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: 1vzt:
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:Mn1369 b:17.0 occ:1.00 O A:HOH2211 2.1 18.0 1.0 O1B A:UDP1370 2.2 13.0 1.0 OD1 A:ASP227 2.2 15.8 1.0 OD2 A:ASP225 2.2 12.5 1.0 O1A A:UDP1370 2.3 15.2 1.0 OD2 A:ASP227 2.5 16.2 1.0 CG A:ASP227 2.7 16.1 1.0 CG A:ASP225 3.2 14.6 1.0 PB A:UDP1370 3.4 17.7 1.0 PA A:UDP1370 3.4 17.4 1.0 O3A A:UDP1370 3.4 16.8 1.0 CB A:ASP225 3.5 14.7 1.0 O3B A:UDP1370 3.7 15.8 1.0 O3' A:UDP1370 3.8 17.7 1.0 NZ A:LYS359 3.8 14.6 1.0 O A:HOH2215 4.0 15.0 1.0 CB A:ASP227 4.2 15.7 1.0 O A:HOH2203 4.2 17.3 1.0 O A:HOH2217 4.2 26.7 1.0 O5' A:UDP1370 4.3 17.4 1.0 OD1 A:ASP225 4.3 16.1 1.0 C5' A:UDP1370 4.4 16.3 1.0 O A:HOH2212 4.5 15.8 1.0 O A:HOH2111 4.5 18.0 1.0 O A:HOH2200 4.5 16.4 1.0 C3' A:UDP1370 4.5 17.2 1.0 O2B A:UDP1370 4.6 17.4 1.0 O2A A:UDP1370 4.6 16.7 1.0 CB A:ALA282 4.7 11.3 1.0 O A:ASP227 4.8 15.3 1.0 C4' A:UDP1370 4.9 16.7 1.0 CA A:ASP225 4.9 15.0 1.0 N A:ASP227 4.9 13.4 1.0 CA A:ASP227 5.0 14.7 1.0 N A:TRS1371 5.0 34.3 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:Mn2369 b:19.2 occ:1.00 OD1 B:ASP1227 2.1 16.1 1.0 O1B B:UDP2370 2.1 13.7 1.0 O B:HOH2221 2.2 14.4 1.0 OD2 B:ASP1225 2.3 13.5 1.0 O1A B:UDP2370 2.3 16.6 1.0 OD2 B:ASP1227 2.4 15.4 1.0 CG B:ASP1227 2.6 15.3 1.0 CG B:ASP1225 3.3 14.1 1.0 PB B:UDP2370 3.3 17.6 1.0 PA B:UDP2370 3.4 18.6 1.0 O3A B:UDP2370 3.4 14.7 1.0 CB B:ASP1225 3.5 13.6 1.0 O3B B:UDP2370 3.8 14.6 1.0 NZ B:LYS1359 3.8 11.3 1.0 O3' B:UDP2370 3.8 18.0 1.0 O B:HOH2225 3.9 18.9 1.0 CB B:ASP1227 4.1 17.1 1.0 O B:HOH2208 4.2 17.5 1.0 O5' B:UDP2370 4.3 14.9 1.0 O B:HOH2093 4.3 17.7 1.0 O B:HOH2090 4.4 33.4 1.0 OD1 B:ASP1225 4.4 16.4 1.0 O B:HOH2095 4.5 13.9 1.0 C5' B:UDP2370 4.5 15.6 1.0 O B:HOH2202 4.5 16.7 1.0 C3' B:UDP2370 4.6 17.4 1.0 O2B B:UDP2370 4.6 19.3 1.0 O2A B:UDP2370 4.6 17.4 1.0 CB B:ALA1282 4.7 11.1 1.0 O B:ASP1227 4.8 15.5 1.0 N B:ASP1227 4.9 15.2 1.0 CA B:ASP1227 4.9 16.0 1.0 C4' B:UDP2370 4.9 14.8 1.0 CA B:ASP1225 4.9 14.6 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