3BMQ
Structure of Pteridine Reductase 1 (PTR1) from Trypanosoma brucei in ternary complex with cofactor (NADP+) and inhibitor (Compound AX5)
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 | 7 |
| Details | BINDING SITE FOR RESIDUE ACT B 269 |
| Chain | Residue |
| B | ALA212 |
| B | MET213 |
| B | GLY214 |
| B | GLU215 |
| B | HOH405 |
| B | HOH412 |
| B | HOH425 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT C 269 |
| Chain | Residue |
| C | HOH385 |
| B | TYR34 |
| C | HOH380 |
| site_id | AC3 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAP A 269 |
| Chain | Residue |
| A | ARG14 |
| A | ILE15 |
| A | TYR34 |
| A | HIS35 |
| A | ASN36 |
| A | SER37 |
| A | ALA61 |
| A | ASP62 |
| A | LEU63 |
| A | THR64 |
| A | ASN93 |
| A | ALA94 |
| A | SER95 |
| A | THR126 |
| A | LEU159 |
| A | CYS160 |
| A | TYR174 |
| A | LYS178 |
| A | PRO204 |
| A | GLY205 |
| A | SER207 |
| A | LEU208 |
| A | HOH279 |
| A | HOH285 |
| A | HOH288 |
| A | HOH290 |
| A | HOH321 |
| A | HOH337 |
| A | HOH342 |
| A | HOH431 |
| A | HOH436 |
| A | HOH445 |
| A | HOH576 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE AX5 A 270 |
| Chain | Residue |
| A | ARG14 |
| A | SER95 |
| A | PHE97 |
| A | ASP161 |
| A | TYR174 |
| A | LEU208 |
| A | PRO210 |
| A | HOH576 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE DTT A 271 |
| Chain | Residue |
| A | ASP161 |
| A | MET163 |
| A | TYR174 |
| A | GLY205 |
| A | TRP221 |
| A | HOH350 |
| A | HOH366 |
| site_id | AC6 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAP B 270 |
| 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 | HOH366 |
| B | HOH383 |
| B | HOH385 |
| B | HOH416 |
| B | HOH438 |
| B | HOH439 |
| B | HOH466 |
| B | HOH524 |
| B | HOH637 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE AX5 B 271 |
| Chain | Residue |
| B | ARG14 |
| B | SER95 |
| B | PHE97 |
| B | TYR174 |
| B | LEU208 |
| B | PRO210 |
| B | HOH732 |
| site_id | AC8 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAP C 270 |
| Chain | Residue |
| 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 | HOH280 |
| C | HOH289 |
| C | HOH290 |
| C | HOH292 |
| C | HOH314 |
| C | HOH325 |
| C | HOH340 |
| C | HOH434 |
| C | HOH445 |
| C | HOH527 |
| C | HOH584 |
| C | ARG14 |
| C | ILE15 |
| C | HIS33 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE AX5 C 271 |
| Chain | Residue |
| C | ARG14 |
| C | SER95 |
| C | PHE97 |
| C | ASP161 |
| C | TYR174 |
| C | LEU208 |
| C | LEU209 |
| C | PRO210 |
| site_id | BC1 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAP D 269 |
| 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 | HOH591 |
| D | HOH603 |
| D | HOH608 |
| D | HOH617 |
| D | HOH658 |
| D | HOH659 |
| D | HOH759 |
| D | HOH767 |
| D | HOH784 |
| D | HOH842 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE AX5 D 270 |
| Chain | Residue |
| D | ARG14 |
| D | SER95 |
| D | PHE97 |
| D | TYR174 |
| D | LEU208 |
| D | LEU209 |
| D | PRO210 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DTT D 271 |
| Chain | Residue |
| D | PHE97 |
| D | ASP161 |
| D | GLY205 |
| D | TRP221 |
| D | HOH678 |
| D | HOH718 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 272 |
| Chain | Residue |
| B | HIS267 |
| C | MET163 |
| C | GLN166 |
| C | PRO167 |
| C | CYS168 |
| C | GLY205 |
| C | TRP221 |
| C | HOH360 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 273 |
| Chain | Residue |
| C | PHE97 |
| C | ASP161 |
| C | CYS168 |
| C | HOH322 |
| C | HOH408 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 272 |
| Chain | Residue |
| B | ASP161 |
| B | HOH471 |
| B | HOH511 |
| B | HOH729 |
| B | HOH730 |
| B | HOH731 |
| B | HOH732 |
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 | |
| B | ASP161-ALA189 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | ASP165 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | PHE171 | |
| C | LYS178 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | PHE171 | |
| A | LYS178 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | PHE171 | |
| D | LYS178 |
| site_id | CSA13 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | TYR174 | |
| B | LYS178 |
| site_id | CSA14 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | TYR174 | |
| C | LYS178 |
| site_id | CSA15 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR174 | |
| A | LYS178 |
| site_id | CSA16 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | TYR174 | |
| D | LYS178 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | ASP165 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | ASP165 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | ASP165 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | SER152 | |
| B | TYR174 | |
| B | LYS178 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | SER152 | |
| C | TYR174 | |
| C | LYS178 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | SER152 | |
| A | TYR174 | |
| A | LYS178 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | SER152 | |
| D | TYR174 | |
| D | LYS178 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | PHE171 | |
| B | LYS178 |
| site_id | MCSA1 |
| 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 | MCSA2 |
| 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 |
