Calcium in PDB 7pul: Crystal Structure of Endoglycosidase E GH20 Domain From Enterococcus Faecalis

Enzymatic activity of Crystal Structure of Endoglycosidase E GH20 Domain From Enterococcus Faecalis

All present enzymatic activity of Crystal Structure of Endoglycosidase E GH20 Domain From Enterococcus Faecalis:
3.2.1.52;

Protein crystallography data

The structure of Crystal Structure of Endoglycosidase E GH20 Domain From Enterococcus Faecalis, PDB code: 7pul was solved by M.Garcia-Alija, J.J.Du, B.Trastoy, E.J.Sundberg, M.Guerin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.08 / 1.40
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 39.298, 57.046, 69.525, 90, 92.97, 90
R / Rfree (%) 15.8 / 18.3

Other elements in 7pul:

The structure of Crystal Structure of Endoglycosidase E GH20 Domain From Enterococcus Faecalis also contains other interesting chemical elements:

Magnesium (Mg) 3 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Endoglycosidase E GH20 Domain From Enterococcus Faecalis (pdb code 7pul). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Endoglycosidase E GH20 Domain From Enterococcus Faecalis, PDB code: 7pul:

Calcium binding site 1 out of 1 in 7pul

Go back to Calcium Binding Sites List in 7pul
Calcium binding site 1 out of 1 in the Crystal Structure of Endoglycosidase E GH20 Domain From Enterococcus Faecalis


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Endoglycosidase E GH20 Domain From Enterococcus Faecalis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca901

b:13.4
occ:1.00
 OE1 A:GLN771 2.3 12.6 1.0
O A:HOH1181 2.4 22.8 1.0
OD2 A:ASP774 2.4 15.0 1.0
O A:HOH1201 2.4 22.0 1.0
OD1 A:ASP773 2.4 13.7 1.0
OD2 A:ASP773 2.4 22.8 1.0
CG A:ASP773 2.8 16.8 1.0
CD A:GLN771 3.4 12.8 1.0
HB2 A:GLN771 3.5 13.4 1.0
CG A:ASP774 3.5 13.2 1.0
HB3 A:GLN771 3.8 13.4 1.0
H A:ASP774 4.0 14.3 1.0
HA A:ASP766 4.0 19.3 1.0
O A:HOH1015 4.0 25.2 1.0
HE22 A:GLN771 4.0 16.6 1.0
CB A:GLN771 4.0 11.2 1.0
NE2 A:GLN771 4.1 13.8 1.0
OD1 A:ASP774 4.2 17.2 1.0
CG A:GLN771 4.3 11.5 1.0
CB A:ASP773 4.3 13.9 1.0
N A:ASP774 4.4 11.9 1.0
O A:HOH1246 4.5 31.5 1.0
CB A:ASP774 4.6 13.8 1.0
HB2 A:ASP774 4.7 16.6 1.0
HB2 A:ASP773 4.7 16.7 1.0
O A:ASP766 4.7 19.6 1.0
HB3 A:ASP773 4.8 16.7 1.0
H A:ASP773 4.8 15.6 1.0
CA A:ASP766 4.8 16.1 1.0
HG3 A:GLN771 4.8 13.8 1.0
HE21 A:GLN771 4.9 16.6 1.0
C A:ASP766 4.9 20.1 1.0
HG2 A:GLN771 5.0 13.8 1.0
CA A:ASP774 5.0 12.5 1.0

Reference:

M.Garcia-Alija, J.J.Du, I.Ordonez, A.Diz-Vallenilla, A.Moraleda-Montoya, N.Sultana, C.G.Huynh, C.Li, T.C.Donahue, L.X.Wang, B.Trastoy, E.J.Sundberg, M.E.Guerin. Mechanism of Cooperative N-Glycan Processing By the Multi-Modular Endoglycosidase Endoe. Nat Commun V. 13 1137 2022.
ISSN: ESSN 2041-1723
PubMed: 35241669
DOI: 10.1038/S41467-022-28722-W
Page generated: Fri Jul 19 03:18:39 2024

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