3MCV
Structure of PTR1 from Trypanosoma brucei in ternary complex with 2,4-diamino-5-[2-(2,5-dimethoxyphenyl)ethyl]thieno[2,3-d]-pyrimidine and NADP+
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 | 33 |
| Details | BINDING SITE FOR RESIDUE NAP A 269 |
| 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 | SER207 |
| A | LEU208 |
| A | MCV300 |
| A | HOH306 |
| A | HOH307 |
| A | HOH321 |
| A | HOH331 |
| A | HOH362 |
| A | HOH368 |
| A | TYR34 |
| A | HOH383 |
| A | HOH409 |
| A | HOH448 |
| A | HOH454 |
| A | HIS35 |
| A | ASN36 |
| A | SER37 |
| A | ALA61 |
| A | ASP62 |
| A | LEU63 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE MCV A 300 |
| Chain | Residue |
| A | ARG14 |
| A | SER95 |
| A | PHE97 |
| A | ASP161 |
| A | CYS168 |
| A | TYR174 |
| A | GLY205 |
| A | MET213 |
| A | TRP221 |
| A | NAP269 |
| A | HOH409 |
| A | HOH510 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT A 270 |
| Chain | Residue |
| A | ARG222 |
| A | ARG230 |
| A | GLU231 |
| A | HOH388 |
| A | HOH519 |
| site_id | AC4 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAP B 269 |
| 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 | SER207 |
| B | LEU208 |
| B | MCV300 |
| B | HOH303 |
| B | HOH307 |
| B | HOH315 |
| B | HOH337 |
| B | HOH339 |
| B | HOH348 |
| B | HOH374 |
| B | HOH381 |
| B | HOH493 |
| B | HOH512 |
| B | HOH513 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE MCV B 300 |
| Chain | Residue |
| B | ARG14 |
| B | SER95 |
| B | PHE97 |
| B | TYR174 |
| B | GLY205 |
| B | VAL206 |
| B | MET213 |
| B | TRP221 |
| B | NAP269 |
| B | HOH386 |
| B | HOH493 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 270 |
| Chain | Residue |
| B | HOH399 |
| B | HOH425 |
| B | ALA212 |
| B | MET213 |
| B | GLY214 |
| B | GLU215 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 271 |
| Chain | Residue |
| B | TYR34 |
| B | VAL58 |
| C | VAL57 |
| C | VAL58 |
| C | HOH418 |
| site_id | AC8 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAP C 269 |
| 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 | SER207 |
| C | LEU208 |
| C | MCV300 |
| C | HOH314 |
| C | HOH315 |
| C | HOH341 |
| C | HOH357 |
| C | HOH364 |
| C | HOH373 |
| C | HOH393 |
| C | HOH394 |
| C | HOH395 |
| C | HOH435 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE MCV C 300 |
| Chain | Residue |
| C | ARG14 |
| C | SER95 |
| C | PHE97 |
| C | ASP161 |
| C | CYS168 |
| C | TYR174 |
| C | GLY205 |
| C | VAL206 |
| C | PRO210 |
| C | MET213 |
| C | TRP221 |
| C | NAP269 |
| C | HOH364 |
| site_id | BC1 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAP D 269 |
| Chain | Residue |
| D | LYS13 |
| 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 | SER207 |
| D | LEU208 |
| D | MCV300 |
| D | HOH304 |
| D | HOH305 |
| D | HOH328 |
| D | HOH348 |
| D | HOH360 |
| D | HOH376 |
| D | HOH402 |
| D | HOH439 |
| D | HOH459 |
| site_id | BC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE MCV D 300 |
| Chain | Residue |
| D | ARG14 |
| D | SER95 |
| D | PHE97 |
| D | ASP161 |
| D | CYS168 |
| D | TYR174 |
| D | GLY205 |
| D | VAL206 |
| D | MET213 |
| D | TRP221 |
| D | NAP269 |
| D | HOH439 |
| D | HOH487 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT D 270 |
| Chain | Residue |
| A | HIS267 |
| D | CYS168 |
| D | MET169 |
| D | TRP221 |
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 |
