3IX9
Crystal structure of Streptococcus pneumoniae dihydrofolate reductase - Sp9 mutant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004146 | molecular_function | dihydrofolate reductase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046452 | biological_process | dihydrofolate metabolic process |
| A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| A | 0046655 | biological_process | folic acid metabolic process |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0050661 | molecular_function | NADP binding |
| B | 0004146 | molecular_function | dihydrofolate reductase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006730 | biological_process | one-carbon metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046452 | biological_process | dihydrofolate metabolic process |
| B | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| B | 0046655 | biological_process | folic acid metabolic process |
| B | 0046677 | biological_process | response to antibiotic |
| B | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NDP A 193 |
| Chain | Residue |
| A | TRP9 |
| A | VAL48 |
| A | THR49 |
| A | LEU66 |
| A | THR67 |
| A | ARG68 |
| A | HIS81 |
| A | VAL100 |
| A | GLY101 |
| A | GLY102 |
| A | LYS103 |
| A | ALA10 |
| A | GLN104 |
| A | ILE105 |
| A | HOH176 |
| A | HOH182 |
| A | MTX200 |
| A | HOH208 |
| A | HOH222 |
| A | HOH270 |
| A | HOH275 |
| A | HOH277 |
| A | ILE17 |
| A | HOH281 |
| A | HOH297 |
| A | HOH308 |
| A | GLY18 |
| A | ASN21 |
| A | ARG22 |
| A | LEU23 |
| A | GLY46 |
| A | ARG47 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE MTX A 200 |
| Chain | Residue |
| A | ILE8 |
| A | TRP9 |
| A | LEU23 |
| A | GLU30 |
| A | GLN32 |
| A | PHE34 |
| A | LYS35 |
| A | ARG61 |
| A | VAL100 |
| A | HOH187 |
| A | HOH190 |
| A | HOH192 |
| A | NDP193 |
| A | HOH206 |
| A | HOH207 |
| A | HOH215 |
| A | HOH330 |
| site_id | AC3 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NDP B 193 |
| Chain | Residue |
| A | ASN40 |
| A | HOH185 |
| A | HOH210 |
| A | HOH218 |
| B | TRP9 |
| B | ALA10 |
| B | ILE17 |
| B | GLY18 |
| B | LYS19 |
| B | ASN21 |
| B | ARG22 |
| B | LEU23 |
| B | TRP25 |
| B | GLY46 |
| B | ARG47 |
| B | VAL48 |
| B | THR49 |
| B | LEU66 |
| B | THR67 |
| B | ARG68 |
| B | HIS81 |
| B | VAL100 |
| B | GLY101 |
| B | GLY102 |
| B | LYS103 |
| B | GLN104 |
| B | ILE105 |
| B | HOH182 |
| B | HOH187 |
| B | HOH197 |
| B | MTX200 |
| B | HOH205 |
| B | HOH231 |
| B | HOH246 |
| B | HOH277 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE MTX B 200 |
| Chain | Residue |
| B | NDP193 |
| B | HOH236 |
| B | HOH244 |
| A | HOH280 |
| B | ILE8 |
| B | TRP9 |
| B | LEU23 |
| B | PRO28 |
| B | GLU30 |
| B | LEU31 |
| B | GLN32 |
| B | PHE34 |
| B | LYS35 |
| B | ARG56 |
| B | ARG61 |
| B | VAL100 |
| B | THR119 |
| B | HOH188 |
Functional Information from PROSITE/UniProt
| site_id | PS00075 |
| Number of Residues | 23 |
| Details | DHFR_1 Dihydrofolate reductase (DHFR) domain signature. VIGkdnrLPWylpa.ElqhFketT |
| Chain | Residue | Details |
| A | VAL16-THR38 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 322 |
| Details | Domain: {"description":"DHFR","evidences":[{"source":"PROSITE-ProRule","id":"PRU00660","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 46 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
