6GEX
Trypanosoma brucei PTR1 in complex with inhibitor 2h (F246)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0047040 | molecular_function | pteridine reductase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0047040 | molecular_function | pteridine reductase activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0047040 | molecular_function | pteridine reductase activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0047040 | molecular_function | pteridine reductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| 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 | SER207 |
| A | LEU208 |
| A | EWK302 |
| A | HOH404 |
| A | HOH407 |
| A | HOH411 |
| A | HOH436 |
| A | HOH443 |
| A | HOH454 |
| A | TYR34 |
| A | HOH491 |
| A | HOH498 |
| A | HOH522 |
| A | HIS35 |
| A | ASN36 |
| A | SER37 |
| A | ALA61 |
| A | ASP62 |
| A | LEU63 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue EWK A 302 |
| Chain | Residue |
| A | SER95 |
| A | PHE97 |
| A | CYS168 |
| A | TYR174 |
| A | MET213 |
| A | TRP221 |
| A | NAP301 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue ACT A 303 |
| Chain | Residue |
| A | LYS13 |
| A | ARG14 |
| A | ARG17 |
| A | HOH417 |
| A | HOH418 |
| site_id | AC4 |
| Number of Residues | 30 |
| Details | binding site for residue NAP B 301 |
| 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 | EWK302 |
| B | HOH418 |
| B | HOH422 |
| B | HOH425 |
| B | HOH442 |
| B | HOH448 |
| B | HOH482 |
| B | HOH524 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue EWK B 302 |
| Chain | Residue |
| B | SER95 |
| B | PHE97 |
| B | CYS168 |
| B | TYR174 |
| B | MET213 |
| B | TRP221 |
| B | NAP301 |
| B | HOH557 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | binding site for residue GOL B 303 |
| Chain | Residue |
| B | VAL42 |
| B | ALA45 |
| B | ASP46 |
| B | ASN49 |
| B | ALA56 |
| B | VAL57 |
| B | VAL58 |
| B | HOH414 |
| C | TYR34 |
| C | VAL58 |
| C | CYS59 |
| C | GLN60 |
| C | HOH417 |
| site_id | AC7 |
| Number of Residues | 30 |
| Details | binding site for residue NAP C 301 |
| Chain | Residue |
| C | ASN36 |
| C | SER37 |
| 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 | HOH404 |
| C | HOH412 |
| C | HOH420 |
| C | HOH432 |
| C | HOH435 |
| C | HOH446 |
| C | HOH493 |
| C | HOH495 |
| C | ARG14 |
| C | ILE15 |
| C | TYR34 |
| C | HIS35 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue ACT C 302 |
| Chain | Residue |
| B | TYR34 |
| B | VAL58 |
| C | VAL57 |
| C | VAL58 |
| C | HOH417 |
| site_id | AC9 |
| Number of Residues | 32 |
| 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 | ASP161 |
| D | TYR174 |
| D | LYS178 |
| D | PRO204 |
| D | GLY205 |
| D | SER207 |
| D | LEU208 |
| D | EWK302 |
| D | HOH411 |
| D | HOH432 |
| D | HOH433 |
| D | HOH436 |
| D | HOH487 |
| D | HOH488 |
| D | HOH514 |
| D | HOH521 |
| site_id | AD1 |
| Number of Residues | 9 |
| Details | binding site for residue EWK D 302 |
| Chain | Residue |
| D | SER95 |
| D | PHE97 |
| D | PRO99 |
| 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 |
