4HOG
Candida glabrata dihydrofolate reductase complexed with NADPH and 5-[3-(2-methoxy-4-phenylphenyl)but-1-yn-1-yl]-6-methylpyrimidine-2,4-diamine (UCP111H)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004146 | molecular_function | dihydrofolate reductase activity |
A | 0005575 | cellular_component | cellular_component |
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 | 0000166 | molecular_function | nucleotide binding |
B | 0004146 | molecular_function | dihydrofolate reductase activity |
B | 0005575 | cellular_component | cellular_component |
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 | 31 |
Details | BINDING SITE FOR RESIDUE NDP A 301 |
Chain | Residue |
A | VAL10 |
A | ARG56 |
A | LYS57 |
A | THR58 |
A | VAL77 |
A | SER78 |
A | ARG79 |
A | ASN96 |
A | SER97 |
A | LEU98 |
A | ILE121 |
A | ALA11 |
A | GLY123 |
A | GLY124 |
A | GLU125 |
A | ILE126 |
A | TYR127 |
A | GLN129 |
A | 18H302 |
A | CL304 |
A | HOH410 |
A | HOH427 |
A | ILE19 |
A | HOH454 |
A | HOH484 |
A | GLY20 |
A | PHE21 |
A | GLY23 |
A | ASN24 |
A | LEU25 |
A | GLY55 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 18H A 302 |
Chain | Residue |
A | ILE9 |
A | VAL10 |
A | ALA11 |
A | GLU32 |
A | MET33 |
A | PHE36 |
A | THR58 |
A | SER61 |
A | PRO63 |
A | PHE66 |
A | ILE121 |
A | TYR127 |
A | THR140 |
A | NDP301 |
A | HOH427 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 303 |
Chain | Residue |
A | ARG79 |
B | SER97 |
B | LEU98 |
B | ARG99 |
B | NDP301 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 304 |
Chain | Residue |
A | SER97 |
A | LEU98 |
A | ARG99 |
A | NDP301 |
B | ARG79 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 305 |
Chain | Residue |
A | ARG37 |
A | ARG72 |
site_id | AC6 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE NDP B 301 |
Chain | Residue |
A | CL303 |
B | VAL10 |
B | ALA11 |
B | ILE19 |
B | GLY20 |
B | GLY23 |
B | ASN24 |
B | LEU25 |
B | GLY55 |
B | ARG56 |
B | LYS57 |
B | THR58 |
B | VAL77 |
B | SER78 |
B | ARG79 |
B | ASN96 |
B | SER97 |
B | LEU98 |
B | ILE121 |
B | GLY122 |
B | GLY123 |
B | GLY124 |
B | GLU125 |
B | ILE126 |
B | TYR127 |
B | GLN129 |
B | 18H302 |
B | HOH412 |
B | HOH413 |
B | HOH444 |
B | HOH474 |
site_id | AC7 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE 18H B 302 |
Chain | Residue |
B | TYR127 |
B | THR140 |
B | NDP301 |
B | ILE9 |
B | VAL10 |
B | ALA11 |
B | ARG28 |
B | GLU32 |
B | MET33 |
B | PHE36 |
B | ILE62 |
B | PRO63 |
B | ILE121 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL B 303 |
Chain | Residue |
B | ARG37 |
B | ARG72 |
Functional Information from PROSITE/UniProt
site_id | PS00075 |
Number of Residues | 23 |
Details | DHFR_1 Dihydrofolate reductase (DHFR) domain signature. GIGfqgnLPWrlak.EmkyFrevT |
Chain | Residue | Details |
A | GLY18-THR40 |