4CM8
Crystal structure of pteridine reductase 1 (PTR1) from Trypanosoma brucei in ternary complex with cofactor and inhibitor
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 1269 |
| 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 | IZ91270 |
| A | HOH2008 |
| A | HOH2009 |
| A | HOH2010 |
| A | HOH2013 |
| A | HOH2017 |
| A | HOH2049 |
| A | TYR34 |
| A | HOH2054 |
| A | HOH2154 |
| A | HOH2157 |
| A | HOH2298 |
| A | HOH2300 |
| A | HIS35 |
| A | ASN36 |
| A | SER37 |
| A | ALA61 |
| A | ASP62 |
| A | LEU63 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAP B 1269 |
| 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 | IZ91270 |
| B | HOH2008 |
| B | HOH2009 |
| B | HOH2010 |
| B | HOH2023 |
| B | HOH2060 |
| B | HOH2068 |
| B | HOH2073 |
| B | HOH2156 |
| B | HOH2289 |
| site_id | AC3 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAP C 1269 |
| 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 | IZ91270 |
| C | HOH2009 |
| C | HOH2010 |
| C | HOH2011 |
| C | HOH2019 |
| C | HOH2047 |
| C | HOH2053 |
| C | HOH2131 |
| C | HOH2134 |
| C | HOH2238 |
| C | HOH2240 |
| site_id | AC4 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAP D 1269 |
| 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 | IZ91270 |
| D | HOH2005 |
| D | HOH2006 |
| D | HOH2007 |
| D | HOH2018 |
| D | HOH2045 |
| D | HOH2051 |
| D | HOH2114 |
| D | HOH2204 |
| D | HOH2205 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE IZ9 A 1270 |
| Chain | Residue |
| A | ARG14 |
| A | SER95 |
| A | PHE97 |
| A | ASP161 |
| A | MET163 |
| A | CSX168 |
| A | TYR174 |
| A | GLY205 |
| A | PRO210 |
| A | TRP221 |
| A | NAP1269 |
| A | DTT1272 |
| A | HOH2017 |
| D | HIS267 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE IZ9 B 1270 |
| Chain | Residue |
| B | ARG14 |
| B | SER95 |
| B | PHE97 |
| B | ASP161 |
| B | MET163 |
| B | GLN166 |
| B | CYS168 |
| B | TYR174 |
| B | GLY205 |
| B | PRO210 |
| B | TRP221 |
| B | NAP1269 |
| B | DTT1271 |
| B | HOH2023 |
| B | HOH2195 |
| C | HIS267 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE IZ9 C 1270 |
| Chain | Residue |
| B | HIS267 |
| C | ARG14 |
| C | SER95 |
| C | PHE97 |
| C | ASP161 |
| C | MET163 |
| C | GLN166 |
| C | CSX168 |
| C | TYR174 |
| C | PRO210 |
| C | TRP221 |
| C | NAP1269 |
| C | GOL1272 |
| C | HOH2019 |
| C | HOH2163 |
| C | HOH2171 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE IZ9 D 1270 |
| Chain | Residue |
| A | HIS267 |
| D | ARG14 |
| D | SER95 |
| D | PHE97 |
| D | ASP161 |
| D | MET163 |
| D | GLN166 |
| D | CSX168 |
| D | TYR174 |
| D | PRO210 |
| D | TRP221 |
| D | NAP1269 |
| D | GOL1271 |
| D | HOH2018 |
| D | HOH2149 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT A 1271 |
| Chain | Residue |
| A | LYS13 |
| A | ARG14 |
| A | ARG17 |
| A | HOH2015 |
| A | HOH2301 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT C 1271 |
| Chain | Residue |
| B | TYR34 |
| B | VAL58 |
| C | VAL57 |
| C | VAL58 |
| C | HOH2081 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DTT A 1272 |
| Chain | Residue |
| A | PHE97 |
| A | CSX168 |
| A | LEU209 |
| A | IZ91270 |
| A | HOH2302 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE DTT B 1271 |
| Chain | Residue |
| B | PHE97 |
| B | CYS168 |
| B | IZ91270 |
| B | HOH2290 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 1272 |
| Chain | Residue |
| C | CSX168 |
| C | MET213 |
| C | TRP221 |
| C | IZ91270 |
| C | HOH2242 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 1271 |
| Chain | Residue |
| D | PHE97 |
| D | CSX168 |
| D | VAL206 |
| D | MET213 |
| D | TRP221 |
| D | IZ91270 |
| D | HOH2054 |
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 |
| B | ASP161-ALA189 | |
| A | ASP161-ALA189 |
Catalytic Information from CSA
| 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 | LYS178 | 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 |
| D | ARG14 | electrostatic stabiliser, hydrogen bond donor, steric role |
| D | ASP161 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| D | LYS178 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
