2VTK
THYMIDINE KINASE FROM HERPES SIMPLEX VIRUS TYPE 1 IN COMPLEX WITH ADP AND DEOXYTHYMIDINE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004797 | molecular_function | thymidine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006230 | biological_process | TMP biosynthetic process |
A | 0009157 | biological_process | deoxyribonucleoside monophosphate biosynthetic process |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0071897 | biological_process | DNA biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ADP A 400 |
Chain | Residue |
A | GLY59 |
A | GLN331 |
A | HOH615 |
A | MET60 |
A | GLY61 |
A | LYS62 |
A | THR63 |
A | THR64 |
A | ARG216 |
A | ARG220 |
A | ARG222 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE THM A 500 |
Chain | Residue |
A | GLU83 |
A | ILE100 |
A | TYR101 |
A | GLN125 |
A | ALA168 |
A | ARG222 |
A | GLU225 |
A | HOH606 |
A | HOH615 |
A | HOH616 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_04029 |
Chain | Residue | Details |
A | GLU83 |
site_id | SWS_FT_FI2 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04029 |
Chain | Residue | Details |
A | GLY56 | |
A | TYR101 | |
A | GLN125 | |
A | ARG216 | |
A | ARG222 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1kim |
Chain | Residue | Details |
A | GLU83 | |
A | ARG222 | |
A | GLY59 | |
A | ARG163 |
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 588 |
Chain | Residue | Details |
A | LYS62 | electrostatic stabiliser, polar interaction |
A | GLU83 | proton acceptor, proton donor |
A | ASP162 | metal ligand |
A | ARG163 | electrostatic stabiliser, polar interaction |
A | ARG220 | electrostatic stabiliser, polar interaction |
A | ARG222 | electrostatic stabiliser, polar interaction |
A | GLU225 | electrostatic stabiliser, polar interaction |