3F0T
Crystal structure of thymidine kinase from Herpes simplex virus type 1 in complex with N-methyl-DHBT
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 |
| B | 0004797 | molecular_function | thymidine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006230 | biological_process | TMP biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 400 |
| Chain | Residue |
| A | HOH23 |
| A | HIS58 |
| A | GLY59 |
| A | MET60 |
| A | GLY61 |
| A | ARG220 |
| A | ARG222 |
| A | HOH456 |
| A | HOH479 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 401 |
| Chain | Residue |
| A | HIS105 |
| A | ARG226 |
| A | HOH461 |
| B | SER74 |
| B | ARG75 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 402 |
| Chain | Residue |
| A | ARG212 |
| A | ARG216 |
| B | ARG220 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE NCV A 500 |
| Chain | Residue |
| A | HIS58 |
| A | GLN125 |
| A | MET128 |
| A | ARG163 |
| A | ALA168 |
| A | TYR172 |
| A | ARG222 |
| A | HOH425 |
| A | HOH428 |
| A | HOH440 |
| A | HOH456 |
| A | HOH478 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 400 |
| Chain | Residue |
| B | HIS58 |
| B | GLY59 |
| B | MET60 |
| B | GLY61 |
| B | LYS62 |
| B | THR63 |
| B | HOH409 |
| B | HOH412 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 401 |
| Chain | Residue |
| B | HOH42 |
| B | LYS317 |
| B | ARG320 |
| B | HOH379 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 402 |
| Chain | Residue |
| A | ASP211 |
| B | ARG212 |
| B | ARG220 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE NCV B 500 |
| Chain | Residue |
| B | HIS58 |
| B | GLU83 |
| B | TRP88 |
| B | ILE100 |
| B | TYR101 |
| B | GLN125 |
| B | MET128 |
| B | ARG163 |
| B | TYR172 |
| B | ARG176 |
| B | HOH396 |
| B | HOH444 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_04029 |
| Chain | Residue | Details |
| A | GLU83 | |
| B | GLU83 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04029 |
| Chain | Residue | Details |
| A | GLN125 | |
| A | ARG216 | |
| A | ARG222 | |
| B | GLY56 | |
| B | TYR101 | |
| B | GLN125 | |
| B | ARG216 | |
| B | ARG222 | |
| A | GLY56 | |
| A | TYR101 |
Catalytic Information from CSA
| 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 |
