Manganese in PDB 1o7q: 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: 1o7q 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)	40.0 / 1.3
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	45.326, 94.678, 95.006, 90.00, 99.03, 90.00
R / Rfree (%)	10.69 / 15.43

The binding sites of Manganese atom in the Roles of Individual Residues of Alpha-1,3 Galactosyltransferases in Substrate Binding and Catalysis (pdb code 1o7q). 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: 1o7q:
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:Mn1371 b:4.9 occ:1.00 O1B A:UDP1374 2.1 5.8 1.0 OD2 A:ASP225 2.1 5.0 1.0 O A:HOH2453 2.2 6.0 1.0 OD1 A:ASP227 2.2 4.9 1.0 O1A A:UDP1374 2.2 5.1 1.0 OD2 A:ASP227 2.4 5.4 1.0 CG A:ASP227 2.7 5.2 1.0 HB3 A:ASP225 3.2 5.5 1.0 CG A:ASP225 3.2 3.9 1.0 PB A:UDP1374 3.3 5.3 1.0 PA A:UDP1374 3.4 5.2 1.0 HZ1 A:LYS359 3.5 9.4 1.0 O3A A:UDP1374 3.6 4.6 1.0 CB A:ASP225 3.6 4.6 1.0 HZ2 A:LYS359 3.7 9.4 1.0 O3B A:UDP1374 3.7 6.2 1.0 HZ3 A:LYS359 3.8 9.4 1.0 NZ A:LYS359 3.8 6.3 1.0 O3' A:UDP1374 3.9 5.2 1.0 HB2 A:ASP225 3.9 5.5 1.0 O A:HOH2464 3.9 16.3 1.0 HB1 A:ALA282 4.2 7.2 1.0 CB A:ASP227 4.2 4.5 1.0 O A:HOH2455 4.2 8.1 1.0 OD1 A:ASP225 4.3 5.3 1.0 H A:ASP227 4.3 5.3 1.0 C5' A:UDP1374 4.3 5.1 1.0 O5' A:UDP1374 4.4 4.9 1.0 O A:HOH2427 4.4 6.1 1.0 O A:HOH2265 4.5 7.1 1.0 HB3 A:ASP227 4.5 5.4 1.0 O2A A:UDP1374 4.5 5.6 1.0 O2B A:UDP1374 4.5 5.5 1.0 HB2 A:ALA282 4.6 7.2 1.0 O A:HOH2264 4.6 19.0 1.0 O A:HOH2266 4.6 6.1 1.0 HB2 A:ASP227 4.7 5.4 1.0 C3' A:UDP1374 4.7 4.8 1.0 CB A:ALA282 4.8 4.8 1.0 O A:ASP227 4.8 5.6 1.0 C4' A:UDP1374 4.9 4.9 1.0 N A:ASP227 5.0 4.4 1.0 CA A:ASP227 5.0 4.9 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:Mn1369 b:5.1 occ:1.00 O1B B:UDP1376 2.1 5.3 1.0 OD2 B:ASP225 2.1 5.1 1.0 O B:HOH2464 2.2 6.5 1.0 OD1 B:ASP227 2.2 5.0 1.0 O1A B:UDP1376 2.2 5.1 1.0 OD2 B:ASP227 2.4 5.3 1.0 CG B:ASP227 2.7 5.3 1.0 HB3 B:ASP225 3.1 5.0 1.0 CG B:ASP225 3.2 4.1 1.0 PB B:UDP1376 3.3 5.2 1.0 PA B:UDP1376 3.4 5.0 1.0 HZ3 B:LYS359 3.4 11.1 1.0 O3A B:UDP1376 3.6 4.8 1.0 CB B:ASP225 3.6 4.2 1.0 HZ1 B:LYS359 3.7 11.1 1.0 HZ2 B:LYS359 3.7 11.1 1.0 O3B B:UDP1376 3.7 6.1 1.0 O B:HOH2477 3.8 17.2 1.0 NZ B:LYS359 3.8 7.4 1.0 HB2 B:ASP225 3.8 5.0 1.0 O3' B:UDP1376 3.9 5.0 1.0 HB3 B:ALA282 4.1 6.6 1.0 CB B:ASP227 4.2 5.1 1.0 O B:HOH2466 4.2 7.3 1.0 OD1 B:ASP225 4.3 4.9 1.0 H B:ASP227 4.3 5.8 1.0 C5' B:UDP1376 4.4 5.3 1.0 O B:HOH2437 4.4 6.5 1.0 O5' B:UDP1376 4.4 4.8 1.0 HB3 B:ASP227 4.5 6.2 1.0 O B:HOH2270 4.5 7.2 1.0 O2A B:UDP1376 4.5 5.9 1.0 O2B B:UDP1376 4.5 6.2 1.0 HB2 B:ALA282 4.5 6.6 1.0 O B:HOH2269 4.6 20.7 1.0 O B:HOH2271 4.6 6.8 1.0 HB2 B:ASP227 4.7 6.2 1.0 C3' B:UDP1376 4.7 4.6 1.0 CB B:ALA282 4.8 4.4 1.0 O B:ASP227 4.8 5.6 1.0 C4' B:UDP1376 4.9 4.9 1.0 N B:ASP227 5.0 4.8 1.0 CA B:ASP227 5.0 4.5 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