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Calcium in PDB 6pzd: Crystal Structure of the Neuraminidase Stabilization Mutant Y169AH From A/Shanghai/2/2013 (H7N9)

Enzymatic activity of Crystal Structure of the Neuraminidase Stabilization Mutant Y169AH From A/Shanghai/2/2013 (H7N9)

All present enzymatic activity of Crystal Structure of the Neuraminidase Stabilization Mutant Y169AH From A/Shanghai/2/2013 (H7N9):
3.2.1.18;

Protein crystallography data

The structure of Crystal Structure of the Neuraminidase Stabilization Mutant Y169AH From A/Shanghai/2/2013 (H7N9), PDB code: 6pzd was solved by X.Zhu, I.A.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.95 / 1.12
Space group I 4 3 2
Cell size a, b, c (Å), α, β, γ (°) 182.219, 182.219, 182.219, 90.00, 90.00, 90.00
R / Rfree (%) 11.2 / 12.8

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the Neuraminidase Stabilization Mutant Y169AH From A/Shanghai/2/2013 (H7N9) (pdb code 6pzd). 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 the Neuraminidase Stabilization Mutant Y169AH From A/Shanghai/2/2013 (H7N9), PDB code: 6pzd:

Calcium binding site 1 out of 1 in 6pzd

Go back to Calcium Binding Sites List in 6pzd
Calcium binding site 1 out of 1 in the Crystal Structure of the Neuraminidase Stabilization Mutant Y169AH From A/Shanghai/2/2013 (H7N9)


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 the Neuraminidase Stabilization Mutant Y169AH From A/Shanghai/2/2013 (H7N9) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca518

b:9.2
occ:0.53
 O A:ASP293 2.3 10.0 1.0
O A:GLY297 2.4 12.5 1.0
OD2 A:ASP324 2.4 10.6 1.0
O A:HOH761 2.5 12.3 1.0
O A:HOH916 2.5 12.8 1.0
O A:ASN347 2.5 9.4 1.0
HA A:ASN294 3.3 11.7 1.0
CG A:ASP324 3.5 9.3 1.0
HA3 A:GLY348 3.5 9.7 1.0
C A:ASP293 3.5 8.7 1.0
C A:GLY297 3.6 10.4 1.0
HA2 A:GLY348 3.6 9.7 1.0
C A:ASN347 3.7 9.3 1.0
HA A:SER298 3.7 11.1 1.0
O A:HOH1032 3.8 15.4 1.0
CA A:GLY348 3.9 8.1 1.0
HB3 A:ASP324 4.0 10.8 1.0
CA A:ASN294 4.0 9.8 1.0
H A:ASN347 4.1 12.3 1.0
O A:HOH752 4.1 10.0 1.0
H A:GLY297 4.2 13.4 1.0
N A:GLY348 4.2 8.9 1.0
N A:ASN294 4.2 8.9 1.0
CB A:ASP324 4.3 9.0 1.0
HB3 A:ASP293 4.3 11.0 1.0
OD1 A:ASP324 4.3 8.8 1.0
C A:ASN294 4.3 10.4 1.0
HB2 A:ASP324 4.4 10.8 1.0
N A:SER298 4.4 8.9 1.0
HG A:SER298 4.5 13.1 1.0
N A:GLY297 4.5 11.2 1.0
CA A:SER298 4.5 9.2 1.0
H A:ASP293 4.6 9.9 1.0
CA A:GLY297 4.6 11.0 1.0
HG3 A:ARG292 4.6 10.5 1.0
O A:ASN294 4.6 14.5 1.0
OG A:SER298 4.6 10.9 1.0
CA A:ASP293 4.6 8.9 1.0
O A:ASN344 4.8 12.7 1.0
N A:ASN347 4.8 10.2 1.0
N A:ASP293 4.8 8.2 1.0
CA A:ASN347 4.9 10.1 1.0
HA3 A:GLY297 4.9 13.2 1.0
CB A:ASP293 4.9 9.2 1.0
N A:TRP295 4.9 10.5 1.0
OD1 A:ASP293 4.9 12.1 1.0

Reference:

X.Zhu, H.L.Turner, S.Lang, R.Mcbride, S.Bangaru, I.M.Gilchuk, W.Yu, J.C.Paulson, J.E.Crowe Jr., A.B.Ward, I.A.Wilson. Structural Basis of Protection Against H7N9 Influenza Virus By Human Anti-N9 Neuraminidase Antibodies. Cell Host Microbe 2019.
ISSN: ESSN 1934-6069
PubMed: 31757767
DOI: 10.1016/J.CHOM.2019.10.002
Page generated: Tue Jul 16 13:09:05 2024

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