6RXC
Leishmania major pteridine reductase 1 (LmPTR1) in complex with inhibitor 4 (NMT-C0026)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0031427 | biological_process | response to methotrexate |
| A | 0047040 | molecular_function | pteridine reductase activity |
| B | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0031427 | biological_process | response to methotrexate |
| B | 0047040 | molecular_function | pteridine reductase activity |
| C | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0031427 | biological_process | response to methotrexate |
| C | 0047040 | molecular_function | pteridine reductase activity |
| D | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0031427 | biological_process | response to methotrexate |
| D | 0047040 | molecular_function | pteridine reductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | binding site for residue NDP A 301 |
| Chain | Residue |
| A | GLY13 |
| A | ASP65 |
| A | LEU66 |
| A | ASN109 |
| A | ALA110 |
| A | SER111 |
| A | SER112 |
| A | ASP142 |
| A | MET179 |
| A | VAL180 |
| A | ASP181 |
| A | ARG17 |
| A | TYR194 |
| A | LYS198 |
| A | PRO224 |
| A | GLY225 |
| A | SER227 |
| A | KMK302 |
| A | HOH411 |
| A | HOH422 |
| A | HOH425 |
| A | HOH433 |
| A | LEU18 |
| A | HOH443 |
| A | HOH445 |
| A | HOH454 |
| A | HIS36 |
| A | TYR37 |
| A | HIS38 |
| A | ARG39 |
| A | SER40 |
| A | ALA64 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue KMK A 302 |
| Chain | Residue |
| A | SER111 |
| A | PHE113 |
| A | ASP181 |
| A | TYR191 |
| A | TYR194 |
| A | LEU226 |
| A | LEU229 |
| A | NDP301 |
| A | HOH402 |
| A | HOH413 |
| B | KMK302 |
| site_id | AC3 |
| Number of Residues | 28 |
| Details | binding site for residue NDP B 301 |
| Chain | Residue |
| B | ARG17 |
| B | LEU18 |
| B | TYR37 |
| B | HIS38 |
| B | ARG39 |
| B | SER40 |
| B | ASP65 |
| B | LEU66 |
| B | ASN109 |
| B | ALA110 |
| B | SER111 |
| B | SER112 |
| B | ASP142 |
| B | MET179 |
| B | VAL180 |
| B | ASP181 |
| B | TYR194 |
| B | LYS198 |
| B | PRO224 |
| B | GLY225 |
| B | SER227 |
| B | KMK302 |
| B | HOH407 |
| B | HOH411 |
| B | HOH419 |
| B | HOH437 |
| B | HOH460 |
| B | HOH464 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue KMK B 302 |
| Chain | Residue |
| A | KMK302 |
| B | SER111 |
| B | PHE113 |
| B | ASP181 |
| B | LEU188 |
| B | TYR194 |
| B | MET233 |
| B | VAL237 |
| B | NDP301 |
| B | HOH420 |
| B | HOH432 |
| C | ARG287 |
| site_id | AC5 |
| Number of Residues | 31 |
| Details | binding site for residue NDP C 301 |
| Chain | Residue |
| C | TYR194 |
| C | LYS198 |
| C | PRO224 |
| C | GLY225 |
| C | LEU226 |
| C | SER227 |
| C | KMK302 |
| C | HOH425 |
| C | HOH428 |
| C | HOH457 |
| C | HOH464 |
| C | HOH483 |
| C | HOH485 |
| C | HOH488 |
| C | HOH490 |
| C | ARG17 |
| C | LEU18 |
| C | TYR37 |
| C | HIS38 |
| C | ARG39 |
| C | SER40 |
| C | ALA64 |
| C | ASP65 |
| C | LEU66 |
| C | ASN109 |
| C | ALA110 |
| C | SER111 |
| C | SER112 |
| C | ASP142 |
| C | VAL180 |
| C | ASP181 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue KMK C 302 |
| Chain | Residue |
| C | SER111 |
| C | PHE113 |
| C | ASP181 |
| C | TYR191 |
| C | TYR194 |
| C | GLY225 |
| C | LEU226 |
| C | LEU229 |
| C | VAL230 |
| C | NDP301 |
| C | HOH412 |
| C | HOH484 |
| site_id | AC7 |
| Number of Residues | 26 |
| Details | binding site for residue NDP D 301 |
| Chain | Residue |
| D | ARG17 |
| D | LEU18 |
| D | HIS36 |
| D | TYR37 |
| D | HIS38 |
| D | ARG39 |
| D | SER40 |
| D | ALA64 |
| D | ASP65 |
| D | LEU66 |
| D | SER67 |
| D | ASN109 |
| D | ALA110 |
| D | SER111 |
| D | SER112 |
| D | ASP142 |
| D | MET179 |
| D | VAL180 |
| D | ASP181 |
| D | TYR194 |
| D | LYS198 |
| D | PRO224 |
| D | GLY225 |
| D | SER227 |
| D | KMK302 |
| D | HOH404 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | binding site for residue KMK D 302 |
| Chain | Residue |
| D | SER111 |
| D | PHE113 |
| D | ASP181 |
| D | TYR191 |
| D | TYR194 |
| D | LEU226 |
| D | LEU229 |
| D | VAL237 |
| D | NDP301 |
| D | HOH414 |
| D | HOH431 |
| D | HOH448 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. DamtnqpllgYtiYTMAKGALeGLTrSAA |
| Chain | Residue | Details |
| B | ASP181-ALA209 | |
| A | ASP181-ALA209 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| B | TYR194 | |
| D | TYR194 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| B | ARG17 | |
| D | ARG17 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11373620 |
| Chain | Residue | Details |
| B | SER175 | |
| D | SER175 |
