6HNC
Trypanosoma brucei PTR1 in complex with cycloguanil
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 | LEU63 |
| A | THR64 |
| A | ASN93 |
| A | ALA94 |
| A | SER95 |
| A | THR126 |
| A | LEU159 |
| A | CYS160 |
| A | ASP161 |
| A | TYR174 |
| A | ILE15 |
| A | LYS178 |
| A | PRO204 |
| A | GLY205 |
| A | VAL206 |
| A | SER207 |
| A | LEU208 |
| A | 1CY302 |
| A | GOL304 |
| A | HOH412 |
| A | HOH413 |
| A | HIS33 |
| A | HOH419 |
| A | HOH423 |
| A | HOH481 |
| A | HOH499 |
| A | HOH519 |
| A | TYR34 |
| A | HIS35 |
| A | ASN36 |
| A | SER37 |
| A | ALA61 |
| A | ASP62 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue 1CY A 302 |
| Chain | Residue |
| A | ARG14 |
| A | SER95 |
| A | PHE97 |
| A | TYR174 |
| A | VAL206 |
| A | TRP221 |
| A | NAP301 |
| A | GOL304 |
| A | HOH473 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue ACT A 303 |
| Chain | Residue |
| A | LYS258 |
| A | HOH409 |
| A | HOH442 |
| A | HOH448 |
| C | GLN186 |
| C | GLY254 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 304 |
| Chain | Residue |
| A | SER95 |
| A | ALA96 |
| A | PHE97 |
| A | NAP301 |
| A | 1CY302 |
| A | HOH423 |
| A | HOH510 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue DMS A 305 |
| Chain | Residue |
| A | GLN186 |
| A | GLY254 |
| A | ILE256 |
| A | HOH504 |
| C | LYS258 |
| C | HOH409 |
| C | HOH563 |
| site_id | AC6 |
| Number of Residues | 34 |
| 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 | VAL206 |
| B | SER207 |
| B | LEU208 |
| B | 1CY302 |
| B | HOH409 |
| B | HOH420 |
| B | HOH430 |
| B | HOH438 |
| B | HOH449 |
| B | HOH486 |
| B | HOH489 |
| B | HOH501 |
| B | HOH503 |
| B | HOH539 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue 1CY B 302 |
| Chain | Residue |
| B | PHE97 |
| B | TYR174 |
| B | LEU209 |
| B | TRP221 |
| B | NAP301 |
| B | HOH532 |
| B | ARG14 |
| B | SER95 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue ACT B 303 |
| Chain | Residue |
| B | LYS13 |
| B | ARG14 |
| B | ARG17 |
| B | HOH412 |
| B | HOH437 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 304 |
| Chain | Residue |
| B | GLU215 |
| B | LYS218 |
| B | ARG222 |
| B | HOH403 |
| B | HOH485 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 305 |
| Chain | Residue |
| B | ARG230 |
| B | GLU231 |
| B | SER233 |
| B | HOH411 |
| B | HOH523 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 306 |
| Chain | Residue |
| B | ASN65 |
| B | ILE129 |
| B | HOH559 |
| C | ASN65 |
| C | VAL120 |
| C | ALA121 |
| C | HOH482 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue DMS B 307 |
| Chain | Residue |
| B | LYS258 |
| B | HOH462 |
| D | GLN186 |
| D | GLY254 |
| D | ILE256 |
| D | HOH512 |
| site_id | AD4 |
| Number of Residues | 27 |
| Details | binding site for residue NAP C 301 |
| Chain | Residue |
| C | ARG14 |
| C | ILE15 |
| C | TYR34 |
| C | HIS35 |
| 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 | HOH401 |
| C | HOH416 |
| C | HOH418 |
| C | HOH468 |
| C | HOH490 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue ACT C 302 |
| Chain | Residue |
| C | VAL57 |
| C | VAL58 |
| C | HOH413 |
| C | HOH496 |
| D | TYR34 |
| D | VAL58 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue ACT C 303 |
| Chain | Residue |
| C | ARG223 |
| C | LYS224 |
| C | VAL225 |
| C | ARG229 |
| site_id | AD7 |
| Number of Residues | 9 |
| Details | binding site for residue GOL C 304 |
| Chain | Residue |
| C | TYR34 |
| C | GLN60 |
| C | HOH402 |
| C | HOH404 |
| C | HOH406 |
| D | ASP46 |
| D | ALA56 |
| D | VAL57 |
| D | VAL58 |
| site_id | AD8 |
| Number of Residues | 33 |
| Details | binding site for residue NAP D 301 |
| Chain | Residue |
| D | ARG14 |
| D | ILE15 |
| D | HIS33 |
| 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 | 1CY302 |
| D | HOH408 |
| D | HOH413 |
| D | HOH448 |
| D | HOH450 |
| D | HOH458 |
| D | HOH462 |
| D | HOH492 |
| D | HOH549 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue 1CY D 302 |
| Chain | Residue |
| D | ARG14 |
| D | SER95 |
| D | PHE97 |
| D | TYR174 |
| 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 |
