6GCP
Trypanosoma brucei PTR1 in complex with inhibitor 2d (F186)
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 | 34 |
| Details | binding site for residue NAP A 301 |
| 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 | EUK302 |
| A | HOH410 |
| A | HOH415 |
| A | HOH429 |
| A | HOH433 |
| A | HOH434 |
| A | TYR34 |
| A | HOH466 |
| A | HOH486 |
| A | HOH501 |
| A | HOH503 |
| A | HOH535 |
| A | HIS35 |
| A | ASN36 |
| A | SER37 |
| A | ALA61 |
| A | ASP62 |
| A | LEU63 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue EUK A 302 |
| Chain | Residue |
| A | SER95 |
| A | PHE97 |
| A | CYS168 |
| A | PHE171 |
| A | TYR174 |
| A | PRO210 |
| A | MET213 |
| A | TRP221 |
| A | NAP301 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 303 |
| Chain | Residue |
| A | ARG230 |
| A | GLU231 |
| A | SER233 |
| A | HOH416 |
| site_id | AC4 |
| Number of Residues | 32 |
| Details | binding site for residue NAP B 301 |
| Chain | Residue |
| B | ARG14 |
| B | ILE15 |
| B | HIS33 |
| 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 | EUK302 |
| B | HOH422 |
| B | HOH430 |
| B | HOH434 |
| B | HOH447 |
| B | HOH453 |
| B | HOH475 |
| B | HOH501 |
| B | HOH565 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue EUK B 302 |
| Chain | Residue |
| B | SER95 |
| B | PHE97 |
| B | ASP161 |
| B | CYS168 |
| B | TYR174 |
| B | PRO210 |
| B | MET213 |
| B | TRP221 |
| B | NAP301 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue ACT B 303 |
| Chain | Residue |
| B | TYR34 |
| B | VAL58 |
| B | HOH436 |
| B | HOH554 |
| C | VAL57 |
| C | VAL58 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue ACT B 304 |
| Chain | Residue |
| B | HOH442 |
| B | ALA212 |
| B | MET213 |
| B | GLY214 |
| B | GLU215 |
| B | HOH439 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 305 |
| Chain | Residue |
| B | HIS24 |
| B | GLN25 |
| B | GLU47 |
| B | LEU48 |
| B | GLU51 |
| B | HOH405 |
| B | HOH416 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 306 |
| Chain | Residue |
| B | LEU208 |
| B | GLU231 |
| B | HOH414 |
| site_id | AD1 |
| Number of Residues | 32 |
| Details | binding site for residue NAP C 301 |
| 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 | EUK302 |
| C | HOH411 |
| C | HOH420 |
| C | HOH430 |
| C | HOH438 |
| C | HOH439 |
| C | HOH499 |
| C | HOH503 |
| C | HOH535 |
| C | HOH544 |
| site_id | AD2 |
| Number of Residues | 9 |
| Details | binding site for residue EUK C 302 |
| Chain | Residue |
| C | SER95 |
| C | PHE97 |
| C | ASP161 |
| C | CYS168 |
| C | TYR174 |
| C | PRO210 |
| C | MET213 |
| C | TRP221 |
| C | NAP301 |
| site_id | AD3 |
| Number of Residues | 9 |
| Details | binding site for residue GOL C 303 |
| Chain | Residue |
| B | ASP46 |
| B | VAL57 |
| B | VAL58 |
| B | HOH436 |
| C | TYR34 |
| C | VAL58 |
| C | GLN60 |
| C | HOH402 |
| C | HOH457 |
| site_id | AD4 |
| Number of Residues | 33 |
| Details | binding site for residue NAP D 301 |
| 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 | SER207 |
| D | LEU208 |
| D | EUK302 |
| D | HOH415 |
| D | HOH416 |
| D | HOH418 |
| D | HOH424 |
| D | HOH433 |
| D | HOH482 |
| D | HOH515 |
| D | HOH535 |
| D | HOH537 |
| D | HOH538 |
| site_id | AD5 |
| Number of Residues | 8 |
| Details | binding site for residue EUK D 302 |
| Chain | Residue |
| D | SER95 |
| D | PHE97 |
| D | CYS168 |
| D | TYR174 |
| D | PRO210 |
| D | MET213 |
| D | TRP221 |
| D | NAP301 |
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 |
