2KI5
HERPES SIMPLEX TYPE-1 THYMIDINE KINASE IN COMPLEX WITH THE DRUG ACICLOVIR AT 1.9A RESOLUTION
Replaces: 1KI5Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
| A | 0071897 | biological_process | DNA biosynthetic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004797 | molecular_function | thymidine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006230 | biological_process | TMP biosynthetic process |
| B | 0009157 | biological_process | deoxyribonucleoside monophosphate biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0071897 | biological_process | DNA biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 3 |
| Chain | Residue |
| B | HIS58 |
| B | GLY59 |
| B | MET60 |
| B | GLY61 |
| B | LYS62 |
| B | THR63 |
| B | ARG222 |
| B | HOH594 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 4 |
| Chain | Residue |
| A | GLY59 |
| A | MET60 |
| A | GLY61 |
| A | LYS62 |
| A | THR63 |
| A | ARG222 |
| A | HOH696 |
| A | HOH783 |
| A | HIS58 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE AC2 A 1 |
| Chain | Residue |
| A | HIS58 |
| A | GLU83 |
| A | TRP88 |
| A | ILE100 |
| A | TYR101 |
| A | GLN125 |
| A | MET128 |
| A | ARG163 |
| A | TYR172 |
| A | ARG176 |
| A | ARG222 |
| A | GLU225 |
| A | HOH586 |
| A | HOH587 |
| A | HOH589 |
| A | HOH776 |
| A | HOH779 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE AC2 B 2 |
| Chain | Residue |
| B | GLU83 |
| B | TRP88 |
| B | ILE97 |
| B | TYR101 |
| B | GLN125 |
| B | MET128 |
| B | ARG163 |
| B | TYR172 |
| B | ARG222 |
| B | HOH588 |
| B | HOH590 |
| B | HOH778 |
| B | HOH784 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04029","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04029","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
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 | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1kim |
| Chain | Residue | Details |
| B | GLU83 | |
| B | ARG222 | |
| B | GLY59 | |
| B | 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 |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 588 |
| Chain | Residue | Details |
| B | LYS62 | electrostatic stabiliser, polar interaction |
| B | GLU83 | proton acceptor, proton donor |
| B | ASP162 | metal ligand |
| B | ARG163 | electrostatic stabiliser, polar interaction |
| B | ARG220 | electrostatic stabiliser, polar interaction |
| B | ARG222 | electrostatic stabiliser, polar interaction |
| B | GLU225 | electrostatic stabiliser, polar interaction |
