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Manganese in PDB 2rj1: B-Specific Alpha-1,3-Galactosyltransferase (Gtb) G176R Mutant + Udp + H-Antigen Disaccharide

Enzymatic activity of B-Specific Alpha-1,3-Galactosyltransferase (Gtb) G176R Mutant + Udp + H-Antigen Disaccharide

All present enzymatic activity of B-Specific Alpha-1,3-Galactosyltransferase (Gtb) G176R Mutant + Udp + H-Antigen Disaccharide:
2.4.1.37;

Protein crystallography data

The structure of B-Specific Alpha-1,3-Galactosyltransferase (Gtb) G176R Mutant + Udp + H-Antigen Disaccharide, PDB code: 2rj1 was solved by S.V.Evans, J.A.Alfaro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.74 / 1.55
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 52.450, 149.120, 79.640, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 22.9

Manganese Binding Sites:

The binding sites of Manganese atom in the B-Specific Alpha-1,3-Galactosyltransferase (Gtb) G176R Mutant + Udp + H-Antigen Disaccharide (pdb code 2rj1). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the B-Specific Alpha-1,3-Galactosyltransferase (Gtb) G176R Mutant + Udp + H-Antigen Disaccharide, PDB code: 2rj1:

Manganese binding site 1 out of 1 in 2rj1

Go back to Manganese Binding Sites List in 2rj1
Manganese binding site 1 out of 1 in the B-Specific Alpha-1,3-Galactosyltransferase (Gtb) G176R Mutant + Udp + H-Antigen Disaccharide


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of B-Specific Alpha-1,3-Galactosyltransferase (Gtb) G176R Mutant + Udp + H-Antigen Disaccharide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1

b:14.8
occ:1.00
 O3B A:UDP453 2.1 13.9 1.0
OD2 A:ASP211 2.1 12.9 1.0
O1A A:UDP453 2.2 13.7 1.0
O A:HOH630 2.3 14.7 1.0
OD1 A:ASP213 2.3 12.8 1.0
OD2 A:ASP213 2.5 12.0 1.0
CG A:ASP213 2.7 12.0 1.0
CG A:ASP211 3.2 13.3 1.0
PB A:UDP453 3.3 15.9 1.0
PA A:UDP453 3.4 14.8 1.0
O3A A:UDP453 3.5 14.3 1.0
CB A:ASP211 3.6 11.0 1.0
O A:HOH647 3.8 30.5 1.0
O3' A:UDP453 3.8 11.9 1.0
O1B A:UDP453 4.0 16.5 1.0
CB A:ASP213 4.2 11.8 1.0
C5' A:UDP453 4.2 12.7 1.0
NZ A:LYS346 4.2 15.6 1.0
OD1 A:ASP211 4.3 12.0 1.0
O5' A:UDP453 4.3 13.0 1.0
O A:HOH532 4.4 20.6 1.0
O2B A:UDP453 4.5 15.4 1.0
O2A A:UDP453 4.5 14.9 1.0
C3' A:UDP453 4.6 12.1 1.0
O A:HOH498 4.7 17.3 1.0
O A:ASP213 4.8 12.0 1.0
C4' A:UDP453 4.9 12.7 1.0
SD A:MET214 4.9 15.6 1.0
N A:ASP213 5.0 11.9 1.0
O A:HOH484 5.0 17.1 1.0

Reference:

J.A.Alfaro, R.B.Zheng, M.Persson, J.A.Letts, R.Polakowski, Y.Bai, S.N.Borisova, N.O.Seto, T.L.Lowary, M.M.Palcic, S.V.Evans. Abo(H) Blood Group A and B Glycosyltransferases Recognize Substrate Via Specific Conformational Changes. J.Biol.Chem. V. 283 10097 2008.
ISSN: ISSN 0021-9258
PubMed: 18192272
DOI: 10.1074/JBC.M708669200
Page generated: Sat Oct 5 15:08:10 2024

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