1E92
Pteridine reductase 1 from Leishmania major complexed with NADP+ and dihydrobiopterin
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 | 31 |
Details | BINDING SITE FOR RESIDUE NAP A1289 |
Chain | Residue |
A | ARG17 |
A | LEU66 |
A | ASN109 |
A | ALA110 |
A | SER111 |
A | SER112 |
A | ASP142 |
A | MET179 |
A | VAL180 |
A | ASP181 |
A | TYR194 |
A | LEU18 |
A | LYS198 |
A | PRO224 |
A | GLY225 |
A | LEU226 |
A | SER227 |
A | HBI1290 |
A | HOH2002 |
A | HOH2003 |
A | HOH2005 |
A | HOH2070 |
A | HIS36 |
A | HOH2106 |
A | HOH2107 |
A | TYR37 |
A | HIS38 |
A | ARG39 |
A | SER40 |
A | ALA64 |
A | ASP65 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE HBI A1290 |
Chain | Residue |
A | ARG17 |
A | SER111 |
A | PHE113 |
A | ASP181 |
A | TYR194 |
A | LEU226 |
A | NAP1289 |
A | HOH2109 |
D | HOH2100 |
site_id | AC3 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE NAP B1289 |
Chain | Residue |
B | ARG17 |
B | LEU18 |
B | HIS36 |
B | TYR37 |
B | HIS38 |
B | ARG39 |
B | SER40 |
B | ALA64 |
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 | LEU226 |
B | SER227 |
B | HBI1290 |
B | HOH2003 |
B | HOH2058 |
B | HOH2098 |
B | HOH2099 |
B | HOH2100 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE HBI B1290 |
Chain | Residue |
B | ARG17 |
B | SER111 |
B | PHE113 |
B | ASP181 |
B | TYR194 |
B | LEU226 |
B | LEU229 |
B | NAP1289 |
B | HOH2101 |
C | HOH2107 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B1291 |
Chain | Residue |
A | GLY199 |
A | GLU202 |
A | ARG206 |
B | GLY199 |
B | GLU202 |
B | ARG206 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B1292 |
Chain | Residue |
A | ARG20 |
A | THR50 |
B | ARG20 |
B | THR50 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO B1293 |
Chain | Residue |
A | ASN68 |
B | ASN68 |
site_id | AC8 |
Number of Residues | 33 |
Details | BINDING SITE FOR RESIDUE NAP C1289 |
Chain | Residue |
C | ALA64 |
C | ASP65 |
C | LEU66 |
C | ASN109 |
C | ALA110 |
C | SER111 |
C | SER112 |
C | ASP142 |
C | MET179 |
C | VAL180 |
C | ASP181 |
C | TYR194 |
C | LYS198 |
C | PRO224 |
C | GLY225 |
C | LEU226 |
C | SER227 |
C | HBI1290 |
C | HOH2002 |
C | HOH2044 |
C | HOH2068 |
C | HOH2108 |
C | HOH2109 |
C | HOH2110 |
C | HOH2111 |
C | HOH2112 |
C | ARG17 |
C | LEU18 |
C | HIS36 |
C | TYR37 |
C | HIS38 |
C | ARG39 |
C | SER40 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE HBI C1290 |
Chain | Residue |
C | ARG17 |
C | SER111 |
C | PHE113 |
C | ASP181 |
C | TYR194 |
C | LEU226 |
C | NAP1289 |
C | HOH2113 |
C | HOH2114 |
site_id | BC1 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE NAP D1289 |
Chain | Residue |
D | ARG17 |
D | LEU18 |
D | HIS36 |
D | TYR37 |
D | HIS38 |
D | ARG39 |
D | SER40 |
D | ALA64 |
D | ASP65 |
D | LEU66 |
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 | LEU226 |
D | SER227 |
D | HBI1290 |
D | HOH2039 |
D | HOH2103 |
D | HOH2104 |
D | HOH2105 |
D | HOH2106 |
D | HOH2107 |
D | HOH2108 |
site_id | BC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE HBI D1290 |
Chain | Residue |
D | ARG17 |
D | SER111 |
D | PHE113 |
D | ASP181 |
D | TYR194 |
D | LEU226 |
D | NAP1289 |
D | HOH2109 |
D | HOH2110 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO D1291 |
Chain | Residue |
C | GLY199 |
C | GLU202 |
C | ARG206 |
D | GLY199 |
D | GLU202 |
D | ARG206 |
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 |
A | ASP181-ALA209 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | TYR194 | |
B | TYR194 | |
C | TYR194 | |
D | TYR194 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ARG17 | |
B | ARG17 | |
C | ARG17 | |
D | ARG17 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11373620 |
Chain | Residue | Details |
A | SER175 | |
B | SER175 | |
C | SER175 | |
D | SER175 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
A | LYS198 | |
A | TYR191 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
B | LYS198 | |
B | TYR191 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
C | LYS198 | |
C | TYR191 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
D | LYS198 | |
D | TYR191 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
A | LYS198 | |
A | TYR194 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
B | LYS198 | |
B | TYR194 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
C | LYS198 | |
C | TYR194 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
D | LYS198 | |
D | TYR194 |