Chlorine in PDB 8ua5: Crystal Structure of Infected Cell Protein 0 (ICP0) From Herpes Simplex Virus 1 (A636-Q776)

The structure of Crystal Structure of Infected Cell Protein 0 (ICP0) From Herpes Simplex Virus 1 (A636-Q776), PDB code: 8ua5 was solved by S.Lovell, M.Kashipathy, K.P.Battaile, A.Cooper, D.Davido, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.45 / 2.45
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	97.15, 97.15, 76.721, 90, 90, 90
R / Rfree (%)	19.2 / 25.4

The structure of Crystal Structure of Infected Cell Protein 0 (ICP0) From Herpes Simplex Virus 1 (A636-Q776) also contains other interesting chemical elements:

Iodine

(I)

3 atoms

The binding sites of Chlorine atom in the Crystal Structure of Infected Cell Protein 0 (ICP0) From Herpes Simplex Virus 1 (A636-Q776) (pdb code 8ua5). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Infected Cell Protein 0 (ICP0) From Herpes Simplex Virus 1 (A636-Q776), PDB code: 8ua5:

Chlorine binding site 1 out of 1 in the Crystal Structure of Infected Cell Protein 0 (ICP0) From Herpes Simplex Virus 1 (A636-Q776)


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 Infected Cell Protein 0 (ICP0) From Herpes Simplex Virus 1 (A636-Q776) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl801 b:42.4 occ:1.00 NH1 B:ARG694 3.2 43.2 1.0 CD A:ARG642 3.4 56.7 1.0 NE A:ARG642 3.4 59.4 1.0 NH2 B:ARG694 3.5 40.1 1.0 CA B:ALA698 3.8 48.5 1.0 CZ B:ARG694 3.8 40.2 1.0 O B:ALA697 3.9 44.3 1.0 N B:ALA698 4.1 40.6 1.0 C B:ALA697 4.1 44.9 1.0 CB B:ALA698 4.1 45.5 1.0 CZ A:ARG642 4.4 70.0 1.0 CG A:ARG642 4.6 40.5 1.0 CB B:ALA697 4.6 36.1 1.0

E.Mccloskey, M.Kashipathy, A.Cooper, P.Gao, D.K.Johnson, K.P.Battaile, S.Lovell, D.J.Davido. Hsv-1 ICP0 Dimer Domain Adopts A Novel Beta-Barrel Fold. Proteins 2024.
ISSN: ESSN 1097-0134
PubMed: 38372168
DOI: 10.1002/PROT.26673