4CM3
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 | 5 |
| Details | BINDING SITE FOR RESIDUE DTU A 1168 |
| Chain | Residue |
| A | CYS168 |
| A | GLU217 |
| A | TRP221 |
| A | KP21270 |
| A | HOH2098 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE DTU B 1168 |
| Chain | Residue |
| B | CYS168 |
| B | PHE171 |
| B | TRP221 |
| B | HOH2106 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DTU C 1168 |
| Chain | Residue |
| B | HOH2152 |
| C | CYS168 |
| C | TRP221 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DTU D 1168 |
| Chain | Residue |
| A | HOH2157 |
| D | CYS168 |
| D | PHE171 |
| D | TRP221 |
| D | KP21270 |
| D | HOH2070 |
| site_id | AC5 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAP A 1269 |
| 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 | KP21270 |
| A | HOH2005 |
| A | HOH2006 |
| A | HOH2007 |
| A | HOH2020 |
| A | HOH2023 |
| A | HOH2068 |
| A | HOH2113 |
| A | HOH2159 |
| site_id | AC6 |
| Number of Residues | 33 |
| 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 | KP21270 |
| B | HOH2006 |
| B | HOH2007 |
| B | HOH2008 |
| B | HOH2014 |
| B | HOH2028 |
| B | HOH2031 |
| B | HOH2074 |
| B | HOH2154 |
| B | HOH2155 |
| B | HOH2156 |
| site_id | AC7 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAP C 1269 |
| Chain | Residue |
| C | TYR174 |
| C | LYS178 |
| C | PRO204 |
| C | GLY205 |
| C | SER207 |
| C | LEU208 |
| C | KP21270 |
| C | HOH2003 |
| C | HOH2004 |
| C | HOH2005 |
| C | HOH2010 |
| C | HOH2021 |
| C | HOH2053 |
| C | HOH2085 |
| C | HOH2115 |
| C | ARG14 |
| C | ILE15 |
| C | HIS33 |
| 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 |
| site_id | AC8 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAP D 1269 |
| 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 | KP21270 |
| D | HOH2002 |
| D | HOH2003 |
| D | HOH2004 |
| D | HOH2006 |
| D | HOH2008 |
| D | HOH2015 |
| D | HOH2045 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE KP2 A 1270 |
| Chain | Residue |
| A | SER95 |
| A | PHE97 |
| A | TYR174 |
| A | DTU1168 |
| A | NAP1269 |
| A | HOH2011 |
| A | HOH2113 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE KP2 B 1270 |
| Chain | Residue |
| B | SER95 |
| B | PHE97 |
| B | TYR174 |
| B | LEU209 |
| B | NAP1269 |
| B | HOH2014 |
| B | HOH2116 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE KP2 C 1270 |
| Chain | Residue |
| C | SER95 |
| C | PHE97 |
| C | ASP161 |
| C | TYR174 |
| C | PRO210 |
| C | NAP1269 |
| C | HOH2010 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE KP2 D 1270 |
| Chain | Residue |
| D | SER95 |
| D | PHE97 |
| D | TYR174 |
| D | LEU209 |
| D | PRO210 |
| D | DTU1168 |
| D | NAP1269 |
| D | HOH2008 |
| D | HOH2075 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT A 1271 |
| Chain | Residue |
| A | LYS13 |
| A | ARG14 |
| A | ARG17 |
| A | HOH2009 |
| A | HOH2160 |
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 |
