3H4V
Selective screening and design to identify inhibitors of leishmania major pteridine reductase 1
Replaces: 2P8KFunctional 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 |
E | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
E | 0005829 | cellular_component | cytosol |
E | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0031427 | biological_process | response to methotrexate |
E | 0047040 | molecular_function | pteridine reductase activity |
F | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
F | 0005829 | cellular_component | cytosol |
F | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0031427 | biological_process | response to methotrexate |
F | 0047040 | molecular_function | pteridine reductase activity |
G | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
G | 0005829 | cellular_component | cytosol |
G | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0031427 | biological_process | response to methotrexate |
G | 0047040 | molecular_function | pteridine reductase activity |
H | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
H | 0005829 | cellular_component | cytosol |
H | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
H | 0016491 | molecular_function | oxidoreductase activity |
H | 0031427 | biological_process | response to methotrexate |
H | 0047040 | molecular_function | pteridine reductase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE NAP A 300 |
Chain | Residue |
A | ARG17 |
A | LEU66 |
A | SER67 |
A | ASN109 |
A | ALA110 |
A | SER111 |
A | SER112 |
A | ASP142 |
A | MET179 |
A | VAL180 |
A | TYR194 |
A | LEU18 |
A | LYS198 |
A | PRO224 |
A | GLY225 |
A | LEU226 |
A | SER227 |
A | HOH290 |
A | HOH293 |
A | HOH295 |
A | DVP301 |
A | HOH346 |
A | HIS36 |
A | HOH348 |
A | HOH366 |
A | HOH401 |
A | HOH880 |
A | HOH886 |
A | HOH1097 |
A | TYR37 |
A | HIS38 |
A | ARG39 |
A | SER40 |
A | ALA64 |
A | ASP65 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE DVP A 301 |
Chain | Residue |
A | ARG17 |
A | SER111 |
A | PHE113 |
A | LEU188 |
A | TYR194 |
A | MET233 |
A | NAP300 |
A | HOH352 |
A | HOH938 |
A | HOH1000 |
A | HOH1049 |
A | HOH1069 |
A | HOH1097 |
site_id | AC3 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE NAP B 300 |
Chain | Residue |
B | ARG17 |
B | LEU18 |
B | HIS36 |
B | TYR37 |
B | HIS38 |
B | ARG39 |
B | SER40 |
B | ALA64 |
B | ASP65 |
B | LEU66 |
B | SER67 |
B | ASN109 |
B | ALA110 |
B | SER111 |
B | SER112 |
B | ASP142 |
B | MET179 |
B | VAL180 |
B | LYS198 |
B | PRO224 |
B | GLY225 |
B | SER227 |
B | DVP301 |
B | HOH305 |
B | HOH334 |
B | HOH349 |
B | HOH357 |
B | HOH908 |
B | HOH1034 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE DVP B 301 |
Chain | Residue |
B | ARG17 |
B | SER111 |
B | PHE113 |
B | TYR191 |
B | TYR194 |
B | LEU226 |
B | NAP300 |
B | HOH845 |
B | HOH1043 |
C | HOH957 |
site_id | AC5 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE NAP C 300 |
Chain | Residue |
C | ALA110 |
C | SER111 |
C | SER112 |
C | ASP142 |
C | VAL180 |
C | ASP181 |
C | TYR194 |
C | LYS198 |
C | PRO224 |
C | GLY225 |
C | LEU226 |
C | SER227 |
C | DVP301 |
C | HOH313 |
C | HOH327 |
C | HOH334 |
C | HOH345 |
C | HOH392 |
C | ARG17 |
C | LEU18 |
C | HIS36 |
C | TYR37 |
C | HIS38 |
C | ARG39 |
C | SER40 |
C | ALA64 |
C | ASP65 |
C | LEU66 |
C | SER67 |
C | ASN109 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE DVP C 301 |
Chain | Residue |
C | ARG17 |
C | SER111 |
C | PHE113 |
C | LEU188 |
C | TYR191 |
C | TYR194 |
C | HIS241 |
C | NAP300 |
C | HOH351 |
site_id | AC7 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE NAP D 300 |
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 | LEU226 |
D | SER227 |
D | HOH291 |
D | DVP301 |
D | HOH332 |
D | HOH374 |
D | HOH414 |
site_id | AC8 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE DVP D 301 |
Chain | Residue |
D | ARG17 |
D | SER111 |
D | PHE113 |
D | ASP181 |
D | LEU188 |
D | TYR191 |
D | TYR194 |
D | HIS241 |
D | NAP300 |
D | HOH306 |
D | HOH1008 |
site_id | AC9 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE NAP E 300 |
Chain | Residue |
E | LYS16 |
E | ARG17 |
E | LEU18 |
E | HIS36 |
E | TYR37 |
E | HIS38 |
E | ARG39 |
E | SER40 |
E | ALA64 |
E | ASP65 |
E | LEU66 |
E | SER67 |
E | ASN109 |
E | ALA110 |
E | SER111 |
E | SER112 |
E | ASP142 |
E | MET179 |
E | VAL180 |
E | LYS198 |
E | PRO224 |
E | GLY225 |
E | SER227 |
E | DVP301 |
E | HOH503 |
E | HOH505 |
E | HOH537 |
E | HOH558 |
E | HOH564 |
E | HOH657 |
E | HOH978 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DVP E 301 |
Chain | Residue |
E | ARG17 |
E | SER111 |
E | PHE113 |
E | TYR191 |
E | TYR194 |
E | NAP300 |
site_id | BC2 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE NAP F 300 |
Chain | Residue |
F | ARG17 |
F | LEU18 |
F | HIS36 |
F | TYR37 |
F | HIS38 |
F | ARG39 |
F | SER40 |
F | ALA64 |
F | ASP65 |
F | LEU66 |
F | SER67 |
F | ASN109 |
F | ALA110 |
F | SER111 |
F | SER112 |
F | ASP142 |
F | MET179 |
F | VAL180 |
F | ASP181 |
F | TYR194 |
F | LYS198 |
F | PRO224 |
F | GLY225 |
F | LEU226 |
F | SER227 |
F | DVP301 |
F | HOH526 |
F | HOH539 |
F | HOH557 |
F | HOH559 |
F | HOH581 |
F | HOH622 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE DVP F 301 |
Chain | Residue |
F | ARG17 |
F | SER111 |
F | PHE113 |
F | LEU188 |
F | TYR194 |
F | MET233 |
F | NAP300 |
F | HOH549 |
site_id | BC4 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE NAP G 300 |
Chain | Residue |
G | ARG17 |
G | LEU18 |
G | HIS36 |
G | TYR37 |
G | HIS38 |
G | ARG39 |
G | SER40 |
G | ALA64 |
G | ASP65 |
G | LEU66 |
G | SER67 |
G | ASN109 |
G | SER111 |
G | ASP142 |
G | MET179 |
G | VAL180 |
G | ASP181 |
G | LYS198 |
G | SER227 |
G | DVP301 |
G | HOH692 |
G | HOH722 |
G | HOH742 |
G | HOH746 |
G | HOH747 |
G | HOH778 |
site_id | BC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE DVP G 301 |
Chain | Residue |
G | ARG17 |
G | SER111 |
G | PHE113 |
G | LEU188 |
G | TYR194 |
G | GLY225 |
G | LEU226 |
G | NAP300 |
site_id | BC6 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE NAP H 300 |
Chain | Residue |
H | LYS16 |
H | ARG17 |
H | LEU18 |
H | HIS36 |
H | TYR37 |
H | HIS38 |
H | ARG39 |
H | SER40 |
H | LEU66 |
H | SER67 |
H | ASN109 |
H | SER111 |
H | SER112 |
H | ASP142 |
H | SER146 |
H | VAL180 |
H | ASP181 |
H | TYR194 |
H | LYS198 |
H | PRO224 |
H | GLY225 |
H | LEU226 |
H | SER227 |
H | DVP301 |
H | HOH730 |
H | HOH740 |
H | HOH743 |
H | HOH768 |
H | HOH795 |
H | HOH800 |
site_id | BC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE DVP H 301 |
Chain | Residue |
H | ARG17 |
H | SER111 |
H | PHE113 |
H | ASP181 |
H | LEU188 |
H | TYR191 |
H | TYR194 |
H | GLY225 |
H | ASP232 |
H | HIS241 |
H | NAP300 |
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 | 8 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | TYR194 | |
B | TYR194 | |
C | TYR194 | |
D | TYR194 | |
E | TYR194 | |
F | TYR194 | |
G | TYR194 | |
H | TYR194 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ARG17 | |
B | ARG17 | |
C | ARG17 | |
D | ARG17 | |
E | ARG17 | |
F | ARG17 | |
G | ARG17 | |
H | ARG17 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11373620 |
Chain | Residue | Details |
A | SER175 | |
B | SER175 | |
C | SER175 | |
D | SER175 | |
E | SER175 | |
F | SER175 | |
G | SER175 | |
H | 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 | CSA10 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
B | LYS198 | |
B | TYR194 |
site_id | CSA11 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
C | LYS198 | |
C | TYR194 |
site_id | CSA12 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
D | LYS198 | |
D | TYR194 |
site_id | CSA13 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
E | LYS198 | |
E | TYR194 |
site_id | CSA14 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
F | LYS198 | |
F | TYR194 |
site_id | CSA15 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
G | LYS198 | |
G | TYR194 |
site_id | CSA16 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
H | LYS198 | |
H | TYR194 |
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 |
E | LYS198 | |
E | TYR191 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
F | LYS198 | |
F | TYR191 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
G | LYS198 | |
G | TYR191 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
H | LYS198 | |
H | TYR191 |
site_id | CSA9 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
A | LYS198 | |
A | TYR194 |