Manganese in PDB 6bsw: Crystal Structure of Xyloglucan Xylosyltransferase 1 Ternary Form

All present enzymatic activity of Crystal Structure of Xyloglucan Xylosyltransferase 1 Ternary Form:
2.4.2.39;

The structure of Crystal Structure of Xyloglucan Xylosyltransferase 1 Ternary Form, PDB code: 6bsw was solved by A.T.Culbertson, J.J.Ehrlich, J.Choe, R.B.Honzatko, O.A.Zabotina, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.43 / 2.16
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	65.037, 94.889, 145.104, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 22.9

The binding sites of Manganese atom in the Crystal Structure of Xyloglucan Xylosyltransferase 1 Ternary Form (pdb code 6bsw). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of Xyloglucan Xylosyltransferase 1 Ternary Form, PDB code: 6bsw:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of Xyloglucan Xylosyltransferase 1 Ternary Form


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Xyloglucan Xylosyltransferase 1 Ternary Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn501 b:32.0 occ:1.00 OD1 A:ASP229 2.1 39.0 1.0 OD2 A:ASP227 2.2 33.6 1.0 NE2 A:HIS377 2.2 39.4 1.0 O2B A:UDP502 2.2 49.9 1.0 O2A A:UDP502 2.2 60.9 1.0 OD2 A:ASP229 2.5 36.4 1.0 CG A:ASP229 2.6 40.9 1.0 HB3 A:ASP227 2.9 43.8 1.0 CE1 A:HIS377 3.0 38.5 1.0 PA A:UDP502 3.1 39.2 1.0 HE1 A:HIS377 3.1 46.3 1.0 CG A:ASP227 3.1 33.2 1.0 O5' A:UDP502 3.2 61.9 1.0 CD2 A:HIS377 3.3 35.4 1.0 PB A:UDP502 3.3 50.5 1.0 CB A:ASP227 3.4 36.5 1.0 HD2 A:HIS377 3.5 42.5 1.0 O3A A:UDP502 3.5 87.2 1.0 HB2 A:ASP227 3.5 43.8 1.0 HG12 A:VAL379 3.6 45.1 1.0 HO3' A:UDP502 3.8 63.8 1.0 O3B A:UDP502 3.9 45.1 1.0 HA A:VAL379 4.0 41.2 1.0 H A:ASP229 4.1 40.1 1.0 O3' A:UDP502 4.1 53.1 1.0 CB A:ASP229 4.1 35.8 1.0 ND1 A:HIS377 4.2 29.5 1.0 OD1 A:ASP227 4.3 35.8 1.0 CG A:HIS377 4.3 34.5 1.0 O A:HOH629 4.4 42.4 1.0 CG1 A:VAL379 4.5 37.5 1.0 O1A A:UDP502 4.5 55.1 1.0 HB3 A:ASP229 4.5 43.0 1.0 HG13 A:VAL379 4.5 45.1 1.0 H32 A:GOL504 4.6 95.4 1.0 C5' A:UDP502 4.6 63.5 1.0 O1B A:UDP502 4.6 73.7 1.0 O3 A:GOL504 4.6 76.0 1.0 HA3 A:GLY270 4.6 40.3 1.0 HB2 A:ASP229 4.6 43.0 1.0 H4' A:UDP502 4.8 70.2 1.0 N A:ASP229 4.8 33.4 1.0 CA A:VAL379 4.8 34.3 1.0 CA A:ASP227 4.9 34.8 1.0 CA A:ASP229 4.9 33.0 1.0 O A:HOH656 4.9 48.9 1.0 HD1 A:HIS377 4.9 35.5 1.0 HB2 A:ALA230 5.0 38.5 1.0 C A:ASP229 5.0 37.1 1.0 H5'1 A:UDP502 5.0 76.3 1.0 H11 A:GOL504 5.0 0.1 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of Xyloglucan Xylosyltransferase 1 Ternary Form


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Xyloglucan Xylosyltransferase 1 Ternary Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn501 b:35.2 occ:1.00 NE2 B:HIS377 2.1 30.4 1.0 OD2 B:ASP227 2.1 35.8 1.0 O2 B:NO3503 2.2 45.3 1.0 O3B B:UDP502 2.2 47.3 1.0 OD1 B:ASP229 2.2 43.0 1.0 OD2 B:ASP229 2.3 30.1 1.0 CG B:ASP229 2.6 33.3 1.0 HB3 B:ASP227 2.9 42.8 1.0 CE1 B:HIS377 2.9 29.3 1.0 HE1 B:HIS377 3.0 35.3 1.0 CG B:ASP227 3.0 32.3 1.0 N B:NO3503 3.2 68.7 1.0 HB2 B:ASP227 3.2 42.8 1.0 CB B:ASP227 3.2 35.6 1.0 CD2 B:HIS377 3.3 29.6 1.0 PB B:UDP502 3.5 62.7 1.0 HD2 B:HIS377 3.6 35.6 1.0 H5'1 B:UDP502 3.7 67.1 1.0 O3 B:NO3503 3.8 44.0 1.0 O1B B:UDP502 3.9 65.0 1.0 HG22 B:VAL379 3.9 45.1 1.0 O1 B:NO3503 4.0 62.8 1.0 CB B:ASP229 4.1 34.3 1.0 H B:ASP229 4.1 31.3 1.0 O2B B:UDP502 4.1 72.2 1.0 ND1 B:HIS377 4.1 31.1 1.0 HA B:VAL379 4.2 47.0 1.0 OD1 B:ASP227 4.2 36.3 1.0 O3' B:UDP502 4.3 45.8 1.0 HA3 B:GLY270 4.3 35.6 1.0 CG B:HIS377 4.3 29.8 1.0 HB3 B:ASP229 4.4 41.3 1.0 HB2 B:ASP229 4.5 41.3 1.0 O2A B:UDP502 4.6 75.9 1.0 C5' B:UDP502 4.7 55.9 1.0 CA B:ASP227 4.7 34.9 1.0 O3A B:UDP502 4.8 99.2 1.0 N B:ASP229 4.8 26.0 1.0 CG2 B:VAL379 4.8 37.5 1.0 CA B:ASP229 4.9 32.2 1.0 HD1 B:HIS377 4.9 37.4 1.0 HA2 B:GLY270 4.9 35.6 1.0 O B:HOH665 4.9 40.1 1.0 HB2 B:ALA230 5.0 33.4 1.0

A.T.Culbertson, J.J.Ehrlich, J.Y.Choe, R.B.Honzatko, O.A.Zabotina. Structure of Xyloglucan Xylosyltransferase 1 Reveals Simple Steric Rules That Define Biological Patterns of Xyloglucan Polymers. Proc. Natl. Acad. Sci. V. 115 6064 2018U.S.A..
ISSN: ESSN 1091-6490
PubMed: 29784804
DOI: 10.1073/PNAS.1801105115