2C7V
Structure of Trypanosoma brucei pteridine reductase (PTR1) in ternary complex with cofactor and the antifolate methotrexate
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 | 2 |
| Details | BINDING SITE FOR RESIDUE NI A1273 |
| Chain | Residue |
| A | HIS179 |
| C | HIS179 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A1274 |
| Chain | Residue |
| A | GLU215 |
| A | LYS218 |
| A | ARG222 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NI B1273 |
| Chain | Residue |
| B | HIS179 |
| D | HIS179 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B1274 |
| Chain | Residue |
| B | GLU215 |
| B | HOH2159 |
| B | HOH2217 |
| B | MET213 |
| B | GLY214 |
| site_id | AC5 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAP A1271 |
| 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 | MTX1272 |
| A | HOH2008 |
| A | HOH2127 |
| A | HOH2188 |
| A | HOH2189 |
| A | HOH2190 |
| A | HOH2191 |
| A | HOH2192 |
| A | HOH2193 |
| A | HOH2194 |
| A | HOH2195 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE MTX A1272 |
| Chain | Residue |
| A | ARG14 |
| A | SER95 |
| A | PHE97 |
| A | PRO99 |
| A | CAF168 |
| A | TYR174 |
| A | LEU208 |
| A | MET213 |
| A | NAP1271 |
| A | HOH2141 |
| A | HOH2198 |
| A | HOH2199 |
| A | HOH2200 |
| A | HOH2201 |
| A | HOH2202 |
| A | HOH2203 |
| site_id | AC7 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAP B1271 |
| 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 | MTX1272 |
| B | HOH2004 |
| B | HOH2031 |
| B | HOH2142 |
| B | HOH2205 |
| B | HOH2206 |
| B | HOH2207 |
| B | HOH2208 |
| B | HOH2210 |
| site_id | AC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE MTX B1272 |
| Chain | Residue |
| B | LEU208 |
| B | MET213 |
| B | GLU217 |
| B | TRP221 |
| B | NAP1271 |
| B | HOH2139 |
| B | HOH2157 |
| B | HOH2211 |
| B | HOH2212 |
| B | HOH2213 |
| B | HOH2214 |
| B | HOH2215 |
| B | HOH2216 |
| B | ARG14 |
| B | SER95 |
| B | PHE97 |
| B | PRO99 |
| B | CAF168 |
| B | TYR174 |
| site_id | AC9 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAP C1271 |
| 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 | VAL206 |
| C | SER207 |
| C | LEU208 |
| C | MTX1272 |
| C | HOH2117 |
| C | HOH2180 |
| C | HOH2181 |
| C | HOH2183 |
| C | HOH2184 |
| C | HOH2185 |
| C | HOH2186 |
| site_id | BC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE MTX C1272 |
| Chain | Residue |
| C | ARG14 |
| C | SER95 |
| C | PHE97 |
| C | PRO99 |
| C | TYR174 |
| C | LEU208 |
| C | MET213 |
| C | TRP221 |
| C | NAP1271 |
| C | HOH2124 |
| C | HOH2187 |
| C | HOH2188 |
| C | HOH2189 |
| C | HOH2190 |
| C | HOH2191 |
| C | HOH2192 |
| site_id | BC2 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAP D1271 |
| 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 | CYS160 |
| D | TYR174 |
| D | LYS178 |
| D | PRO204 |
| D | GLY205 |
| D | SER207 |
| D | LEU208 |
| D | MTX1272 |
| D | HOH2114 |
| D | HOH2175 |
| D | HOH2176 |
| D | HOH2177 |
| D | HOH2179 |
| D | HOH2181 |
| D | HOH2182 |
| D | HOH2183 |
| site_id | BC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE MTX D1272 |
| Chain | Residue |
| D | ARG14 |
| D | SER95 |
| D | PHE97 |
| D | PRO99 |
| D | TYR174 |
| D | LEU208 |
| D | PRO210 |
| D | MET213 |
| D | TRP221 |
| D | NAP1271 |
| D | HOH2109 |
| D | HOH2184 |
| D | HOH2185 |
| D | HOH2186 |
| D | HOH2187 |
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 | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 16968221 |
| Chain | Residue | Details |
| A | TYR174 | |
| A | ARG14 | |
| A | ASP161 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 16968221 |
| Chain | Residue | Details |
| B | TYR174 | |
| B | ARG14 | |
| B | ASP161 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 16968221 |
| Chain | Residue | Details |
| C | TYR174 | |
| C | ARG14 | |
| C | ASP161 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 16968221 |
| Chain | Residue | Details |
| D | TYR174 | |
| D | ARG14 | |
| D | ASP161 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 237 |
| Chain | Residue | Details |
| A | ARG14 | electrostatic stabiliser, hydrogen bond donor, steric role |
| A | ASP165 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | VAL182 | 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 | ASP165 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | VAL182 | 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 | ASP165 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| C | VAL182 | 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 | ASP165 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| D | VAL182 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
