Bromine in PDB 1ki4: Crystal Structure of Thymidine Kinase From Herpes Simplex Virus Type I Complexed with 5-Bromothienyldeoxyuridine

All present enzymatic activity of Crystal Structure of Thymidine Kinase From Herpes Simplex Virus Type I Complexed with 5-Bromothienyldeoxyuridine:
2.7.1.21;

The structure of Crystal Structure of Thymidine Kinase From Herpes Simplex Virus Type I Complexed with 5-Bromothienyldeoxyuridine, PDB code: 1ki4 was solved by J.N.Champness, M.S.Bennett, F.Wien, R.Visse, W.C.Summers, M.R.Sanderson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	12.00 / 2.34
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	114.100, 116.000, 108.700, 90.00, 90.00, 90.00
R / Rfree (%)	21 / 30.9

The binding sites of Bromine atom in the Crystal Structure of Thymidine Kinase From Herpes Simplex Virus Type I Complexed with 5-Bromothienyldeoxyuridine (pdb code 1ki4). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Crystal Structure of Thymidine Kinase From Herpes Simplex Virus Type I Complexed with 5-Bromothienyldeoxyuridine, PDB code: 1ki4:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Crystal Structure of Thymidine Kinase From Herpes Simplex Virus Type I Complexed with 5-Bromothienyldeoxyuridine


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of Thymidine Kinase From Herpes Simplex Virus Type I Complexed with 5-Bromothienyldeoxyuridine within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1 b:15.5 occ:1.00 BR A:BTD1 0.0 15.5 1.0 C22 A:BTD1 1.8 25.5 1.0 C33 A:BTD1 2.9 26.5 1.0 O A:HIS164 2.9 15.6 1.0 S11 A:BTD1 3.1 25.1 1.0 CD1 A:TYR132 3.4 18.6 1.0 CE1 A:TYR132 3.5 17.6 1.0 CG A:TYR132 3.5 17.6 1.0 CZ A:TYR132 3.7 16.8 1.0 CB A:ALA168 3.7 14.3 1.0 N A:ALA168 3.8 14.0 1.0 CD2 A:TYR132 3.8 16.0 1.0 CB A:ALA167 3.8 17.1 1.0 CE2 A:TYR132 3.8 16.8 1.0 C A:HIS164 4.0 17.6 1.0 C44 A:BTD1 4.1 22.0 1.0 CA A:PRO165 4.2 18.7 1.0 CB A:ARG163 4.2 17.8 1.0 CB A:TYR132 4.2 13.9 1.0 C55 A:BTD1 4.3 20.3 1.0 CA A:ALA168 4.3 10.8 1.0 O A:PRO165 4.3 15.9 1.0 C A:ALA167 4.4 14.9 1.0 OH A:TYR132 4.4 15.1 1.0 CA A:ALA167 4.4 12.7 1.0 C A:PRO165 4.5 17.4 1.0 N A:ALA167 4.5 13.1 1.0 N A:PRO165 4.5 20.3 1.0 O A:MET128 4.6 15.5 1.0 C A:ARG163 4.7 19.7 1.0 O A:ARG163 4.8 20.9 1.0 N A:HIS164 4.8 20.5 1.0 CA A:GLY129 5.0 15.3 1.0 CD A:ARG163 5.0 19.9 1.0

Bromine binding site 2 out of 2 in the Crystal Structure of Thymidine Kinase From Herpes Simplex Virus Type I Complexed with 5-Bromothienyldeoxyuridine


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Crystal Structure of Thymidine Kinase From Herpes Simplex Virus Type I Complexed with 5-Bromothienyldeoxyuridine within 5.0Å range: probe atom residue distance (Å) B Occ B:Br2 b:31.6 occ:1.00 BR B:BTD2 0.0 31.6 1.0 C22 B:BTD2 1.9 22.8 1.0 S11 B:BTD2 2.9 26.5 1.0 C33 B:BTD2 3.1 23.6 1.0 O B:HIS164 3.2 7.9 1.0 CD1 B:TYR132 3.3 14.6 1.0 CG B:TYR132 3.4 12.0 1.0 CE1 B:TYR132 3.4 12.4 1.0 CD2 B:TYR132 3.5 11.6 1.0 CZ B:TYR132 3.5 13.6 1.0 CE2 B:TYR132 3.5 13.7 1.0 CB B:ALA168 3.6 10.4 1.0 CB B:ALA167 3.7 12.8 1.0 N B:ALA168 3.7 8.0 1.0 C B:HIS164 4.0 5.1 1.0 O B:PRO165 4.0 5.8 1.0 CB B:ARG163 4.1 14.2 1.0 C44 B:BTD2 4.2 18.6 1.0 CB B:TYR132 4.3 15.4 1.0 CA B:ALA168 4.3 11.3 1.0 OH B:TYR132 4.3 17.4 1.0 CA B:PRO165 4.3 3.3 1.0 C55 B:BTD2 4.3 17.4 1.0 C B:ALA167 4.3 8.6 1.0 CA B:ALA167 4.4 9.5 1.0 C B:PRO165 4.4 5.8 1.0 N B:ALA167 4.4 11.1 1.0 N B:PRO165 4.5 6.2 1.0 N B:HIS164 4.7 10.0 1.0 C B:ARG163 4.7 9.2 1.0 CA B:GLY129 5.0 4.7 1.0 O B:ARG163 5.0 12.6 1.0 CA B:HIS164 5.0 6.3 1.0 O B:MET128 5.0 12.4 1.0

J.N.Champness, M.S.Bennett, F.Wien, R.Visse, W.C.Summers, P.Herdewijn, E.De Clerq, T.Ostrowski, R.L.Jarvest, M.R.Sanderson. Exploring the Active Site of Herpes Simplex Virus Type-1 Thymidine Kinase By X-Ray Crystallography of Complexes with Aciclovir and Other Ligands. Proteins V. 32 350 1998.
ISSN: ISSN 0887-3585
PubMed: 9715911
DOI: 10.1002/(SICI)1097-0134(19980815)32:3<350::AID-PROT10>3.0.CO;2-8