3QLW
Candida albicans dihydrofolate reductase complexed with NADPH and 5-[3-(2,5-dimethoxyphenyl)prop-1-yn-1-yl]-6-ethylpyrimidine-2,4-diamine (UCP120B)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004146 | molecular_function | dihydrofolate reductase activity |
| A | 0005739 | cellular_component | mitochondrion |
| 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 | 0050661 | molecular_function | NADP binding |
| B | 0004146 | molecular_function | dihydrofolate reductase activity |
| B | 0005739 | cellular_component | mitochondrion |
| 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 | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NDP A 193 |
| Chain | Residue |
| A | VAL10 |
| A | THR58 |
| A | LEU77 |
| A | SER78 |
| A | ARG79 |
| A | SER94 |
| A | ILE112 |
| A | GLY114 |
| A | ALA115 |
| A | GLU116 |
| A | ILE117 |
| A | ALA11 |
| A | TYR118 |
| A | GLU120 |
| A | N22194 |
| A | ILE19 |
| A | GLY23 |
| A | LYS24 |
| A | MET25 |
| A | GLY55 |
| A | ARG56 |
| A | LYS57 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE N22 A 194 |
| Chain | Residue |
| A | ILE9 |
| A | VAL10 |
| A | ALA11 |
| A | MET25 |
| A | GLU32 |
| A | PHE36 |
| A | ILE112 |
| A | TYR118 |
| A | THR133 |
| A | NDP193 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NDP B 193 |
| Chain | Residue |
| B | ALA11 |
| B | ILE19 |
| B | GLY23 |
| B | LYS24 |
| B | MET25 |
| B | ARG30 |
| B | LYS31 |
| B | GLY55 |
| B | ARG56 |
| B | LYS57 |
| B | THR58 |
| B | LEU77 |
| B | SER78 |
| B | ARG79 |
| B | SER94 |
| B | ILE112 |
| B | GLY114 |
| B | ALA115 |
| B | GLU116 |
| B | ILE117 |
| B | TYR118 |
| B | N22194 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE N22 B 194 |
| Chain | Residue |
| B | ILE9 |
| B | VAL10 |
| B | ALA11 |
| B | GLU32 |
| B | PHE36 |
| B | THR58 |
| B | SER61 |
| B | ILE62 |
| B | ILE112 |
| B | TYR118 |
| B | NDP193 |
Functional Information from PROSITE/UniProt
| site_id | PS00075 |
| Number of Residues | 23 |
| Details | DHFR_1 Dihydrofolate reductase (DHFR) domain signature. GIGykgkMPWrlrk.EiryFkdvT |
| Chain | Residue | Details |
| A | GLY18-THR40 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11520201","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11520201","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P0ABQ4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
