Atomistry » Manganese » PDB 5a58-5b49 » 5ajp
Atomistry »
  Manganese »
    PDB 5a58-5b49 »
      5ajp »

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: Tue Dec 15 04:35:25 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy