Chlorine in PDB 6q2p: Crystal Structure of Mouse Viperin Bound to Cytidine Triphosphate and S-Adenosylhomocysteine

Protein crystallography data

The structure of Crystal Structure of Mouse Viperin Bound to Cytidine Triphosphate and S-Adenosylhomocysteine, PDB code: 6q2p was solved by M.K.Fenwick, M.Dong, H.Lin, S.E.Ealick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.77 / 1.45
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 36.483, 142.588, 143.732, 90.00, 90.00, 90.00
R / Rfree (%) 14.1 / 16

Other elements in 6q2p:

The structure of Crystal Structure of Mouse Viperin Bound to Cytidine Triphosphate and S-Adenosylhomocysteine also contains other interesting chemical elements:

Iron (Fe) 8 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Mouse Viperin Bound to Cytidine Triphosphate and S-Adenosylhomocysteine (pdb code 6q2p). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of Mouse Viperin Bound to Cytidine Triphosphate and S-Adenosylhomocysteine, PDB code: 6q2p:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 6q2p

Go back to Chlorine Binding Sites List in 6q2p
Chlorine binding site 1 out of 3 in the Crystal Structure of Mouse Viperin Bound to Cytidine Triphosphate and S-Adenosylhomocysteine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Mouse Viperin Bound to Cytidine Triphosphate and S-Adenosylhomocysteine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl404

b:14.0
occ:1.00
NZ A:LYS297 3.0 27.0 1.0
N A:SER294 3.3 5.5 1.0
O A:HOH621 3.5 16.5 1.0
O A:HOH552 3.5 38.2 1.0
CB A:SER294 3.7 7.0 1.0
O A:PRO292 3.8 7.3 1.0
CB A:PRO292 3.9 8.8 1.0
C A:PRO292 3.9 4.9 1.0
CE2 A:PHE277 3.9 7.2 1.0
OG A:SER294 4.0 9.2 1.0
N A:GLU293 4.0 5.2 1.0
CA A:SER294 4.1 4.9 1.0
CE A:LYS297 4.1 42.5 1.0
C A:GLU293 4.1 5.1 1.0
CA A:GLU293 4.1 7.2 1.0
CG A:LYS297 4.1 15.4 1.0
CG A:PRO292 4.2 8.4 1.0
CD A:LYS297 4.4 21.2 1.0
CD1 A:LEU281 4.4 8.5 1.0
O A:HOH587 4.5 27.7 1.0
CA A:PRO292 4.5 6.6 1.0
CD2 A:PHE277 4.7 7.1 1.0
CB A:LYS297 4.8 10.2 1.0
CZ A:PHE277 4.8 6.2 1.0
OE2 A:GLU278 4.9 15.2 1.0

Chlorine binding site 2 out of 3 in 6q2p

Go back to Chlorine Binding Sites List in 6q2p
Chlorine binding site 2 out of 3 in the Crystal Structure of Mouse Viperin Bound to Cytidine Triphosphate and S-Adenosylhomocysteine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Mouse Viperin Bound to Cytidine Triphosphate and S-Adenosylhomocysteine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl405

b:14.6
occ:1.00
O A:HOH614 3.1 7.9 1.0
NZ A:LYS114 3.2 11.4 1.0
O A:HOH683 3.7 30.9 1.0
CG A:LYS114 3.7 6.7 1.0
CE A:LYS114 3.9 10.3 1.0
CD A:LYS114 4.4 10.1 1.0
O A:LYS114 4.7 9.2 1.0
O A:LEU148 4.8 10.2 1.0
CB A:LYS114 5.0 8.9 1.0

Chlorine binding site 3 out of 3 in 6q2p

Go back to Chlorine Binding Sites List in 6q2p
Chlorine binding site 3 out of 3 in the Crystal Structure of Mouse Viperin Bound to Cytidine Triphosphate and S-Adenosylhomocysteine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Mouse Viperin Bound to Cytidine Triphosphate and S-Adenosylhomocysteine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl405

b:14.9
occ:1.00
O B:HOH860 3.0 29.9 1.0
N B:SER294 3.2 6.4 1.0
O B:HOH598 3.3 19.8 1.0
NZ B:LYS297 3.4 30.3 1.0
CB B:SER294 3.7 8.7 1.0
O B:PRO292 3.8 7.3 1.0
CB B:PRO292 3.9 7.5 1.0
CE2 B:PHE277 3.9 5.5 1.0
C B:PRO292 3.9 6.6 1.0
OG B:SER294 3.9 8.4 1.0
CG B:LYS297 3.9 22.4 1.0
N B:GLU293 4.0 6.1 1.0
CA B:SER294 4.1 5.7 1.0
C B:GLU293 4.1 6.0 1.0
CA B:GLU293 4.1 5.8 1.0
CG B:PRO292 4.2 9.4 1.0
CE B:LYS297 4.3 41.1 1.0
CD1 B:LEU281 4.4 9.9 1.0
CA B:PRO292 4.5 6.0 1.0
O B:HOH579 4.6 22.9 1.0
O B:HOH605 4.7 26.6 1.0
CD2 B:PHE277 4.7 6.8 1.0
CD B:LYS297 4.7 35.9 1.0
CB B:LYS297 4.7 10.5 1.0
CZ B:PHE277 4.8 7.1 1.0
OE2 B:GLU278 4.9 17.8 1.0

Reference:

M.K.Fenwick, D.Su, M.Dong, H.Lin, S.E.Ealick. Structural Basis of Substrate Selectivity of Viperin. Biochemistry 2020.
ISSN: ISSN 0006-2960
PubMed: 31917549
DOI: 10.1021/ACS.BIOCHEM.9B00741
Page generated: Sat Dec 12 13:32:29 2020

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