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Manganese in PDB 2rj7: B-Specific Alpha-1,3-Galactosyltransferase G176R S235G Mutant (Aabb) + Udpgal + Deoxy-Acceptor

Enzymatic activity of B-Specific Alpha-1,3-Galactosyltransferase G176R S235G Mutant (Aabb) + Udpgal + Deoxy-Acceptor

All present enzymatic activity of B-Specific Alpha-1,3-Galactosyltransferase G176R S235G Mutant (Aabb) + Udpgal + Deoxy-Acceptor:
2.4.1.37;

Protein crystallography data

The structure of B-Specific Alpha-1,3-Galactosyltransferase G176R S235G Mutant (Aabb) + Udpgal + Deoxy-Acceptor, PDB code: 2rj7 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) 19.88 / 1.70
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 52.360, 148.650, 79.520, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 21.7

Manganese Binding Sites:

The binding sites of Manganese atom in the B-Specific Alpha-1,3-Galactosyltransferase G176R S235G Mutant (Aabb) + Udpgal + Deoxy-Acceptor (pdb code 2rj7). 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 G176R S235G Mutant (Aabb) + Udpgal + Deoxy-Acceptor, PDB code: 2rj7:

Manganese binding site 1 out of 1 in 2rj7

Go back to Manganese Binding Sites List in 2rj7
Manganese binding site 1 out of 1 in the B-Specific Alpha-1,3-Galactosyltransferase G176R S235G Mutant (Aabb) + Udpgal + Deoxy-Acceptor


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 G176R S235G Mutant (Aabb) + Udpgal + Deoxy-Acceptor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn453

b:19.7
occ:1.00
 O2B A:GDU475 2.0 24.9 1.0
OD2 A:ASP211 2.1 16.7 1.0
O1A A:GDU475 2.2 16.5 1.0
OD1 A:ASP213 2.4 17.1 1.0
OD2 A:ASP213 2.6 21.1 1.0
CG A:ASP213 2.8 15.9 1.0
CG A:ASP211 3.1 13.4 1.0
PB A:GDU475 3.2 23.8 1.0
PA A:GDU475 3.4 19.2 1.0
CB A:ASP211 3.5 14.5 1.0
O3A A:GDU475 3.6 22.6 1.0
O3D A:GDU475 3.7 15.3 1.0
O2' A:GDU475 3.9 33.7 1.0
O1B A:GDU475 4.1 28.8 1.0
NZ A:LYS346 4.2 26.4 1.0
OD1 A:ASP211 4.2 16.2 1.0
O A:HOH640 4.2 28.4 1.0
C5D A:GDU475 4.3 17.1 1.0
CB A:ASP213 4.4 15.7 1.0
O5D A:GDU475 4.4 17.7 1.0
O3B A:GDU475 4.4 30.6 1.0
O2A A:GDU475 4.5 21.2 1.0
C3D A:GDU475 4.5 17.4 1.0
C2' A:GDU475 4.7 33.3 1.0
C3' A:GDU475 4.7 31.0 1.0
O A:HOH562 4.8 22.0 1.0
CB A:ALA268 4.8 12.6 1.0
C4D A:GDU475 4.9 17.6 1.0
SD A:MET214 4.9 17.1 1.0
CA A:ASP211 5.0 14.1 1.0
O A:ASP213 5.0 13.2 1.0
C1' A:GDU475 5.0 32.0 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 15:08:33 2024

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