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Manganese in PDB 5ajp: Crystal Structure of the Active Form of Galnac-T2 in Complex with Udp and the Glycopeptide MUC5AC-13

Enzymatic activity of Crystal Structure of the Active Form of Galnac-T2 in Complex with Udp and the Glycopeptide MUC5AC-13

All present enzymatic activity of Crystal Structure of the Active Form of Galnac-T2 in Complex with Udp and the Glycopeptide MUC5AC-13:
2.4.1.41;

Protein crystallography data

The structure of Crystal Structure of the Active Form of Galnac-T2 in Complex with Udp and the Glycopeptide MUC5AC-13, PDB code: 5ajp was solved by E.Lira-Navarrete, M.Delasrivas, I.Companon, M.C.Pallares, Y.Kong, J.Iglesias-Fernandez, G.J.L.Bernardes, J.M.Peregrina, C.Rovira, P.Bernado, P.Bruscolini, H.Clausen, A.Lostao, F.Corzana, R.Hurtado-Guerrero, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 89.29 / 1.65
Space group I 41
Cell size a, b, c (Å), α, β, γ (°) 87.266, 87.266, 178.590, 90.00, 90.00, 90.00
R / Rfree (%) 15.598 / 18.558

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of the Active Form of Galnac-T2 in Complex with Udp and the Glycopeptide MUC5AC-13 (pdb code 5ajp). 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 Crystal Structure of the Active Form of Galnac-T2 in Complex with Udp and the Glycopeptide MUC5AC-13, PDB code: 5ajp:

Manganese binding site 1 out of 1 in 5ajp

Go back to Manganese Binding Sites List in 5ajp
Manganese binding site 1 out of 1 in the Crystal Structure of the Active Form of Galnac-T2 in Complex with Udp and the Glycopeptide MUC5AC-13


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 the Active Form of Galnac-T2 in Complex with Udp and the Glycopeptide MUC5AC-13 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1572

b:19.3
occ:1.00
 O1B A:UDP1570 2.1 21.7 1.0
O2A A:UDP1570 2.1 21.4 1.0
NE2 A:HIS359 2.2 19.0 1.0
NE2 A:HIS226 2.2 19.0 1.0
OD2 A:ASP224 2.3 21.0 1.0
O A:HOH2257 2.3 21.3 1.0
CE1 A:HIS359 3.1 19.6 1.0
CE1 A:HIS226 3.2 18.8 1.0
PB A:UDP1570 3.2 22.7 1.0
CD2 A:HIS226 3.2 18.2 1.0
CD2 A:HIS359 3.3 18.1 1.0
CG A:ASP224 3.3 21.7 1.0
PA A:UDP1570 3.4 21.7 1.0
O2B A:UDP1570 3.6 23.6 1.0
O3A A:UDP1570 3.6 20.3 1.0
CB A:ASP224 3.8 18.9 1.0
C5' A:UDP1570 4.2 20.5 1.0
ND1 A:HIS359 4.3 19.1 1.0
ND1 A:HIS226 4.3 18.4 1.0
O A:VAL360 4.3 18.2 1.0
O5' A:UDP1570 4.3 19.9 1.0
CG A:HIS226 4.4 18.4 1.0
CG A:HIS359 4.4 17.9 1.0
OD1 A:ASP224 4.4 23.3 1.0
O3B A:UDP1570 4.6 23.5 1.0
O1A A:UDP1570 4.6 22.8 1.0
O A:HOH2391 4.7 21.3 1.0
C3' A:UDP1570 4.8 21.9 1.0
NH2 A:ARG362 4.8 25.2 1.0
C4' A:UDP1570 5.0 20.5 1.0

Reference:

E.Lira-Navarrete, M.Delasrivas, I.Companon, M.C.Pallares, Y.Kong, J.Iglesias-Fernandez, G.J.L.Bernardes, J.M.Peregrina, C.Rovira, P.Bernado, P.Bruscolini, H.Clausen, A.Lostao, F.Corzana, R.Hurtado-Guerrero. Dynamic Interplay Between Catalytic and Lectin Domains of Galnac-Transferases Modulates Protein O- Glycosylation To Be Published.
Page generated: Sat Oct 5 23:24:23 2024

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