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Sodium in PDB 5mqr: Sialidase BT_1020

Enzymatic activity of Sialidase BT_1020

All present enzymatic activity of Sialidase BT_1020:
3.2.1.187;

Protein crystallography data

The structure of Sialidase BT_1020, PDB code: 5mqr was solved by A.Basle, D.Ndeh, A.Rogowski, A.Cartmell, A.S.Luis, I.Venditto, A.Labourel, H.J.Gilbert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.25 / 2.20
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 125.720, 316.998, 90.023, 90.00, 90.00, 90.00
R / Rfree (%) 16.4 / 19.5

Other elements in 5mqr:

The structure of Sialidase BT_1020 also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Sialidase BT_1020 (pdb code 5mqr). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Sialidase BT_1020, PDB code: 5mqr:

Sodium binding site 1 out of 1 in 5mqr

Go back to Sodium Binding Sites List in 5mqr
Sodium binding site 1 out of 1 in the Sialidase BT_1020


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Sialidase BT_1020 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1208

b:31.0
occ:1.00
O A:HOH1861 2.1 31.4 1.0
O A:HOH2035 2.3 35.7 1.0
O A:GLU495 2.5 23.5 1.0
O A:HOH1619 2.5 32.1 1.0
O A:GLN45 2.5 21.9 1.0
OD1 A:ASN496 2.5 27.4 1.0
C A:GLU495 3.5 24.9 1.0
CG A:ASN496 3.6 26.4 1.0
O A:HOH2113 3.7 51.6 1.0
C A:GLN45 3.7 21.7 1.0
CA A:ASN496 3.8 25.3 1.0
N A:ASN496 4.0 24.6 1.0
O A:HOH1375 4.0 32.7 1.0
N A:SER47 4.1 20.8 1.0
CA A:LEU46 4.2 21.0 1.0
O A:HOH2087 4.2 25.9 1.0
CB A:ASN496 4.3 26.6 1.0
O A:HOH1381 4.4 18.5 1.0
O A:HOH2156 4.4 45.3 1.0
N A:LEU46 4.4 21.8 1.0
O A:HOH1316 4.4 41.8 1.0
CB A:GLU495 4.5 29.1 1.0
C A:LEU46 4.5 21.2 1.0
CA A:GLU495 4.6 26.2 1.0
ND2 A:ASN496 4.7 27.2 1.0
CB A:GLN45 4.8 22.2 1.0
CG A:GLU495 4.8 32.6 1.0
CA A:GLN45 4.8 21.9 1.0
CB A:SER47 4.9 21.6 1.0

Reference:

D.Ndeh, A.Rogowski, A.Cartmell, A.S.Luis, A.Basle, J.Gray, I.Venditto, J.Briggs, X.Zhang, A.Labourel, N.Terrapon, F.Buffetto, S.Nepogodiev, Y.Xiao, R.A.Field, Y.Zhu, M.A.O'neill, B.R.Urbanowicz, W.S.York, G.J.Davies, D.W.Abbott, M.C.Ralet, E.C.Martens, B.Henrissat, H.J.Gilbert. Complex Pectin Metabolism By Gut Bacteria Reveals Novel Catalytic Functions. Nature V. 544 65 2017.
ISSN: ISSN 0028-0836
PubMed: 28329766
DOI: 10.1038/NATURE21725
Page generated: Mon Oct 7 22:44:25 2024

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