2X9G
High resolution structure of TbPTR1 in complex with Pemetrexed
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0047040 | molecular_function | pteridine reductase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0047040 | molecular_function | pteridine reductase activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0047040 | molecular_function | pteridine reductase activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0047040 | molecular_function | pteridine reductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NAP A 1269 |
| Chain | Residue |
| A | ARG14 |
| A | THR64 |
| A | ASN93 |
| A | ALA94 |
| A | SER95 |
| A | THR126 |
| A | LEU159 |
| A | CYS160 |
| A | TYR174 |
| A | LYS178 |
| A | PRO204 |
| A | ILE15 |
| A | GLY205 |
| A | VAL206 |
| A | SER207 |
| A | LEU208 |
| A | LYA1270 |
| A | HOH2055 |
| A | HOH2180 |
| A | HOH2246 |
| A | HOH2334 |
| A | HOH2335 |
| A | TYR34 |
| A | HOH2336 |
| A | HOH2337 |
| A | HOH2338 |
| A | HOH2340 |
| A | HOH2341 |
| A | HOH2344 |
| A | HIS35 |
| A | ASN36 |
| A | SER37 |
| A | ALA61 |
| A | ASP62 |
| A | LEU63 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE LYA A 1270 |
| Chain | Residue |
| A | ARG14 |
| A | SER95 |
| A | PHE97 |
| A | PRO99 |
| A | CYS168 |
| A | MET169 |
| A | PHE171 |
| A | TYR174 |
| A | PRO210 |
| A | MET213 |
| A | TRP221 |
| A | NAP1269 |
| A | HOH2268 |
| A | HOH2343 |
| A | HOH2344 |
| D | HIS267 |
| site_id | AC3 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NAP B 1269 |
| Chain | Residue |
| B | ARG14 |
| B | ILE15 |
| B | TYR34 |
| B | HIS35 |
| B | ASN36 |
| B | SER37 |
| B | ALA61 |
| B | ASP62 |
| B | LEU63 |
| B | THR64 |
| B | ASN93 |
| B | ALA94 |
| B | SER95 |
| B | THR126 |
| B | LEU159 |
| B | CYS160 |
| B | TYR174 |
| B | LYS178 |
| B | PRO204 |
| B | GLY205 |
| B | VAL206 |
| B | SER207 |
| B | LEU208 |
| B | LYA1270 |
| B | HOH2201 |
| B | HOH2264 |
| B | HOH2363 |
| B | HOH2370 |
| B | HOH2371 |
| B | HOH2372 |
| B | HOH2374 |
| B | HOH2375 |
| B | HOH2376 |
| B | HOH2377 |
| B | HOH2378 |
| B | HOH2379 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE LYA B 1270 |
| Chain | Residue |
| B | HOH2363 |
| B | HOH2364 |
| B | HOH2365 |
| B | HOH2366 |
| B | HOH2367 |
| B | HOH2368 |
| B | HOH2369 |
| C | HIS267 |
| B | ARG14 |
| B | SER95 |
| B | PHE97 |
| B | PRO99 |
| B | CYS168 |
| B | MET169 |
| B | TYR174 |
| B | MET213 |
| B | TRP221 |
| B | NAP1269 |
| B | HOH2288 |
| B | HOH2362 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 1271 |
| Chain | Residue |
| B | MET213 |
| B | GLY214 |
| B | GLU215 |
| B | HOH2291 |
| B | HOH2380 |
| site_id | AC6 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NAP C 1269 |
| Chain | Residue |
| C | ARG14 |
| C | ILE15 |
| C | TYR34 |
| C | HIS35 |
| C | ASN36 |
| C | SER37 |
| C | ALA61 |
| C | ASP62 |
| C | LEU63 |
| C | THR64 |
| C | ASN93 |
| C | ALA94 |
| C | SER95 |
| C | THR126 |
| C | LEU159 |
| C | CYS160 |
| C | TYR174 |
| C | LYS178 |
| C | PRO204 |
| C | GLY205 |
| C | VAL206 |
| C | SER207 |
| C | LEU208 |
| C | LYA1270 |
| C | HOH2070 |
| C | HOH2240 |
| C | HOH2323 |
| C | HOH2324 |
| C | HOH2325 |
| C | HOH2327 |
| C | HOH2328 |
| C | HOH2329 |
| C | HOH2330 |
| C | HOH2331 |
| C | HOH2332 |
| C | HOH2333 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE LYA C 1270 |
| Chain | Residue |
| B | HIS267 |
| C | ARG14 |
| C | SER95 |
| C | PHE97 |
| C | CYS168 |
| C | MET169 |
| C | PHE171 |
| C | TYR174 |
| C | PRO210 |
| C | MET213 |
| C | TRP221 |
| C | NAP1269 |
| C | HOH2333 |
| site_id | AC8 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAP D 1269 |
| Chain | Residue |
| D | ARG14 |
| D | ILE15 |
| D | TYR34 |
| D | HIS35 |
| D | ASN36 |
| D | SER37 |
| D | ALA61 |
| D | ASP62 |
| D | LEU63 |
| D | THR64 |
| D | ASN93 |
| D | ALA94 |
| D | SER95 |
| D | THR126 |
| D | LEU159 |
| D | CYS160 |
| D | TYR174 |
| D | LYS178 |
| D | PRO204 |
| D | GLY205 |
| D | VAL206 |
| D | SER207 |
| D | LEU208 |
| D | LYA1270 |
| D | HOH2052 |
| D | HOH2165 |
| D | HOH2219 |
| D | HOH2306 |
| D | HOH2307 |
| D | HOH2308 |
| D | HOH2309 |
| D | HOH2312 |
| D | HOH2314 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE LYA D 1270 |
| Chain | Residue |
| A | HIS267 |
| D | ARG14 |
| D | SER95 |
| D | PHE97 |
| D | PRO99 |
| D | CYS168 |
| D | MET169 |
| D | PHE171 |
| D | TYR174 |
| D | PRO210 |
| D | MET213 |
| D | TRP221 |
| D | NAP1269 |
| D | HOH2314 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. DamvdqpcmaFslYNMGKHALvGLTqSAA |
| Chain | Residue | Details |
| A | ASP161-ALA189 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 237 |
| Chain | Residue | Details |
| A | ARG14 | electrostatic stabiliser, hydrogen bond donor, steric role |
| A | ASP161 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | TYR174 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 237 |
| Chain | Residue | Details |
| B | ARG14 | electrostatic stabiliser, hydrogen bond donor, steric role |
| B | ASP161 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | TYR174 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| site_id | MCSA3 |
| Number of Residues | 3 |
| Details | M-CSA 237 |
| Chain | Residue | Details |
| C | ARG14 | electrostatic stabiliser, hydrogen bond donor, steric role |
| C | ASP161 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| C | TYR174 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| site_id | MCSA4 |
| Number of Residues | 3 |
| Details | M-CSA 237 |
| Chain | Residue | Details |
| D | ARG14 | electrostatic stabiliser, hydrogen bond donor, steric role |
| D | ASP161 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| D | TYR174 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
