2QHX
Structure of Pteridine Reductase from Leishmania major complexed with a ligand
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 | 4 |
| Details | BINDING SITE FOR RESIDUE IOD A 1289 |
| Chain | Residue |
| A | ASN68 |
| B | ASN68 |
| B | IOD1288 |
| B | HOH1443 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IOD B 1288 |
| Chain | Residue |
| A | ASN68 |
| A | IOD1289 |
| A | HOH1488 |
| B | ASN68 |
| site_id | AC3 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAP A 1300 |
| Chain | Residue |
| A | LEU18 |
| A | HIS36 |
| A | TYR37 |
| A | HIS38 |
| A | ARG39 |
| A | SER40 |
| A | ALA64 |
| A | ASP65 |
| A | LEU66 |
| A | ASN109 |
| A | ALA110 |
| A | SER111 |
| A | SER112 |
| A | ASP142 |
| A | MET179 |
| A | VAL180 |
| A | ASP181 |
| A | TYR194 |
| A | LYS198 |
| A | PRO224 |
| A | GLY225 |
| A | LEU226 |
| A | SER227 |
| A | FE11301 |
| A | HOH1303 |
| A | HOH1309 |
| A | HOH1322 |
| A | HOH1335 |
| A | HOH1344 |
| A | HOH1361 |
| A | HOH1362 |
| A | HOH1494 |
| A | ARG17 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE FE1 A 1301 |
| Chain | Residue |
| A | ARG17 |
| A | SER111 |
| A | PHE113 |
| A | ASP181 |
| A | LEU188 |
| A | TYR191 |
| A | TYR194 |
| A | LEU226 |
| A | LEU229 |
| A | MET233 |
| A | HIS241 |
| A | NAP1300 |
| A | HOH1387 |
| A | HOH1521 |
| D | HOH1394 |
| site_id | AC5 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAP B 1302 |
| 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 | FE11303 |
| B | HOH1321 |
| B | HOH1322 |
| B | HOH1326 |
| B | HOH1353 |
| B | HOH1358 |
| B | HOH1384 |
| B | HOH1389 |
| B | HOH1450 |
| B | HOH1466 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE FE1 B 1303 |
| Chain | Residue |
| B | HIS241 |
| B | NAP1302 |
| B | HOH1431 |
| B | HOH1478 |
| B | ARG17 |
| B | SER111 |
| B | PHE113 |
| B | PRO115 |
| B | ASP181 |
| B | LEU188 |
| B | TYR191 |
| B | TYR194 |
| B | LEU229 |
| site_id | AC7 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAP C 1304 |
| Chain | Residue |
| C | ARG17 |
| C | LEU18 |
| C | HIS36 |
| 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 | MET179 |
| C | VAL180 |
| C | ASP181 |
| C | TYR194 |
| C | LYS198 |
| C | PRO224 |
| C | GLY225 |
| C | LEU226 |
| C | SER227 |
| C | FE11305 |
| C | HOH1314 |
| C | HOH1321 |
| C | HOH1330 |
| C | HOH1354 |
| C | HOH1372 |
| C | HOH1389 |
| C | HOH1504 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FE1 C 1305 |
| Chain | Residue |
| C | SER111 |
| C | PHE113 |
| C | TYR191 |
| C | TYR194 |
| C | LEU226 |
| C | NAP1304 |
| C | HOH1348 |
| C | HOH1486 |
| site_id | AC9 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAP D 1306 |
| 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 | FE11307 |
| D | HOH1322 |
| D | HOH1327 |
| D | HOH1333 |
| D | HOH1355 |
| D | HOH1385 |
| D | HOH1405 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FE1 D 1307 |
| Chain | Residue |
| D | ARG17 |
| D | SER111 |
| D | PHE113 |
| D | TYR191 |
| D | TYR194 |
| D | LEU226 |
| D | NAP1306 |
| D | HOH1430 |
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 | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 92 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11373620","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
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 |
