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Zinc in PDB 3d0h: Crystal Structure of Spike Protein Receptor-Binding Domain From the 2002-2003 Sars Coronavirus Civet Strain Complexed with Human-Civet Chimeric Receptor ACE2

Enzymatic activity of Crystal Structure of Spike Protein Receptor-Binding Domain From the 2002-2003 Sars Coronavirus Civet Strain Complexed with Human-Civet Chimeric Receptor ACE2

All present enzymatic activity of Crystal Structure of Spike Protein Receptor-Binding Domain From the 2002-2003 Sars Coronavirus Civet Strain Complexed with Human-Civet Chimeric Receptor ACE2:
3.4.17.23;

Protein crystallography data

The structure of Crystal Structure of Spike Protein Receptor-Binding Domain From the 2002-2003 Sars Coronavirus Civet Strain Complexed with Human-Civet Chimeric Receptor ACE2, PDB code: 3d0h was solved by F.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.50 / 3.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 80.352, 119.841, 109.420, 90.00, 95.89, 90.00
R / Rfree (%) 22.1 / 30.2

Other elements in 3d0h:

The structure of Crystal Structure of Spike Protein Receptor-Binding Domain From the 2002-2003 Sars Coronavirus Civet Strain Complexed with Human-Civet Chimeric Receptor ACE2 also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Spike Protein Receptor-Binding Domain From the 2002-2003 Sars Coronavirus Civet Strain Complexed with Human-Civet Chimeric Receptor ACE2 (pdb code 3d0h). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Spike Protein Receptor-Binding Domain From the 2002-2003 Sars Coronavirus Civet Strain Complexed with Human-Civet Chimeric Receptor ACE2, PDB code: 3d0h:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 3d0h

Go back to Zinc Binding Sites List in 3d0h
Zinc binding site 1 out of 2 in the Crystal Structure of Spike Protein Receptor-Binding Domain From the 2002-2003 Sars Coronavirus Civet Strain Complexed with Human-Civet Chimeric Receptor ACE2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Spike Protein Receptor-Binding Domain From the 2002-2003 Sars Coronavirus Civet Strain Complexed with Human-Civet Chimeric Receptor ACE2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn901

b:0.1
occ:1.00
 NE2 A:HIS374 2.8 58.0 1.0
NE2 A:HIS378 2.8 52.7 1.0
OE2 A:GLU375 3.0 61.1 1.0
OE1 A:GLU402 3.0 56.5 1.0
CD2 A:HIS374 3.1 57.3 1.0
CD2 A:HIS378 3.4 51.8 1.0
OE1 A:GLU375 3.4 59.5 1.0
CD A:GLU375 3.6 59.2 1.0
CE1 A:HIS378 3.8 53.0 1.0
CD A:GLU402 3.9 57.2 1.0
CE1 A:HIS374 4.0 58.0 1.0
OE2 A:GLU402 4.2 59.3 1.0
CG A:HIS378 4.4 49.9 1.0
CG A:HIS374 4.4 56.0 1.0
ND1 A:HIS378 4.6 51.6 1.0
ND1 A:HIS374 4.8 56.8 1.0

Zinc binding site 2 out of 2 in 3d0h

Go back to Zinc Binding Sites List in 3d0h
Zinc binding site 2 out of 2 in the Crystal Structure of Spike Protein Receptor-Binding Domain From the 2002-2003 Sars Coronavirus Civet Strain Complexed with Human-Civet Chimeric Receptor ACE2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Spike Protein Receptor-Binding Domain From the 2002-2003 Sars Coronavirus Civet Strain Complexed with Human-Civet Chimeric Receptor ACE2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn901

b:0.6
occ:1.00
 OE1 B:GLU402 2.4 48.0 1.0
NE2 B:HIS374 2.7 52.5 1.0
NE2 B:HIS378 2.9 48.2 1.0
OE2 B:GLU375 3.3 57.2 1.0
CD B:GLU402 3.4 48.3 1.0
CD2 B:HIS374 3.4 52.4 1.0
CD2 B:HIS378 3.5 48.2 1.0
OE2 B:GLU402 3.6 49.4 1.0
OE1 B:GLU375 3.8 56.7 1.0
CE1 B:HIS378 3.8 47.8 1.0
CE1 B:HIS374 3.9 53.2 1.0
CD B:GLU375 4.0 55.8 1.0
CG B:HIS378 4.6 46.6 1.0
CG B:HIS374 4.6 52.6 1.0
O B:HOH905 4.7 34.4 1.0
CG B:GLU402 4.7 47.1 1.0
ND1 B:HIS378 4.7 47.0 1.0
ND1 B:HIS374 4.9 53.4 1.0

Reference:

F.Li, F.Li. N/A N/A.
ISSN: ISSN 0022-538X
PubMed: 18448527
DOI: 10.1128/JVI.00442-08
Page generated: Thu Oct 24 12:00:26 2024

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