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Zinc in PDB 1zv8: A Structure-Based Mechanism of Sars Virus Membrane Fusion

Protein crystallography data

The structure of A Structure-Based Mechanism of Sars Virus Membrane Fusion, PDB code: 1zv8 was solved by Y.Deng, J.Liu, Q.Zheng, W.Yong, J.Dai, M.Lu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 70.71 / 1.94
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 31.054, 55.565, 71.678, 81.26, 87.08, 84.10
R / Rfree (%) 20.3 / 27.4

Zinc Binding Sites:

The binding sites of Zinc atom in the A Structure-Based Mechanism of Sars Virus Membrane Fusion (pdb code 1zv8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the A Structure-Based Mechanism of Sars Virus Membrane Fusion, PDB code: 1zv8:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1zv8

Go back to Zinc Binding Sites List in 1zv8
Zinc binding site 1 out of 2 in the A Structure-Based Mechanism of Sars Virus Membrane Fusion


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of A Structure-Based Mechanism of Sars Virus Membrane Fusion within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Zn204

b:44.4
occ:1.00
O1 G:CAC201 1.7 37.2 1.0
O G:SER50 2.2 20.1 1.0
C G:SER50 3.0 20.3 1.0
OXT G:SER50 3.2 21.4 1.0
AS G:CAC201 3.3 40.1 1.0
OD2 H:ASP1 3.6 34.3 1.0
C2 G:CAC201 3.7 33.4 1.0
O G:HOH218 4.0 42.6 1.0
CA G:SER50 4.4 19.8 1.0
C1 G:CAC201 4.5 25.3 1.0
O2 G:CAC201 4.7 31.4 1.0
CG H:ASP1 4.8 2.0 1.0
CB G:SER50 4.9 19.2 1.0

Zinc binding site 2 out of 2 in 1zv8

Go back to Zinc Binding Sites List in 1zv8
Zinc binding site 2 out of 2 in the A Structure-Based Mechanism of Sars Virus Membrane Fusion


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of A Structure-Based Mechanism of Sars Virus Membrane Fusion within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Zn203

b:38.5
occ:1.00
O2 G:CAC201 1.8 31.4 1.0
O H:HOH211 1.8 37.5 1.0
O H:ACT202 2.3 52.4 1.0
O H:HOH212 2.5 44.1 1.0
N H:ASP1 3.1 22.8 1.0
C H:ACT202 3.2 51.1 1.0
AS G:CAC201 3.2 40.1 1.0
OXT H:ACT202 3.3 52.1 1.0
C1 G:CAC201 3.4 25.3 1.0
O G:HOH218 4.2 42.6 1.0
O1 G:CAC201 4.4 37.2 1.0
OD1 H:ASP1 4.4 21.9 1.0
CA H:ASP1 4.5 19.1 1.0
CH3 H:ACT202 4.6 54.0 1.0
C2 G:CAC201 4.8 33.4 1.0
CG H:ASP1 4.9 2.0 1.0

Reference:

Y.Deng, J.Liu, Q.Zheng, W.Yong, M.Lu. Structures and Polymorphic Interactions of Two Heptad-Repeat Regions of the Sars Virus S2 Protein. Structure V. 14 889 2006.
ISSN: ISSN 0969-2126
PubMed: 16698550
DOI: 10.1016/J.STR.2006.03.007
Page generated: Sat Sep 26 00:45:01 2020
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