4H97
Candida albicans dihydrofolate reductase complexed with NADPH and 5-{3-[3-methoxy-5-(4-methylphenyl)phenyl]but-1-yn-1-yl}-6-methylpyrimidine-2,4-diamine (UCP111D4M)
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 | 23 |
Details | BINDING SITE FOR RESIDUE NDP A 201 |
Chain | Residue |
A | VAL10 |
A | LYS57 |
A | THR58 |
A | LEU77 |
A | SER78 |
A | ARG79 |
A | SER94 |
A | ILE112 |
A | GLY113 |
A | GLY114 |
A | ALA115 |
A | ALA11 |
A | GLU116 |
A | ILE117 |
A | TYR118 |
A | 53S202 |
A | ILE19 |
A | GLY20 |
A | GLY23 |
A | LYS24 |
A | MET25 |
A | GLY55 |
A | ARG56 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 53S A 202 |
Chain | Residue |
A | ILE9 |
A | VAL10 |
A | ALA11 |
A | GLU32 |
A | ILE33 |
A | PHE36 |
A | THR58 |
A | PRO63 |
A | ILE112 |
A | TYR118 |
A | NDP201 |
site_id | AC3 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NDP B 201 |
Chain | Residue |
B | VAL10 |
B | ALA11 |
B | ILE19 |
B | GLY23 |
B | LYS24 |
B | MET25 |
B | ARG30 |
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 | GLU120 |
B | 53S202 |
B | HOH302 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE 53S B 202 |
Chain | Residue |
B | ILE9 |
B | VAL10 |
B | GLU32 |
B | ILE33 |
B | PHE36 |
B | THR58 |
B | SER61 |
B | PRO63 |
B | PHE66 |
B | ILE112 |
B | TYR118 |
B | NDP201 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL B 203 |
Chain | Residue |
A | ILE85 |
B | ARG28 |
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 |