3FFS
The Crystal Structure of Cryptosporidium parvum Inosine-5'-Monophosphate Dehydrogenase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003938 | molecular_function | IMP dehydrogenase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006177 | biological_process | GMP biosynthetic process |
| A | 0006183 | biological_process | GTP biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003938 | molecular_function | IMP dehydrogenase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006177 | biological_process | GMP biosynthetic process |
| B | 0006183 | biological_process | GTP biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0003938 | molecular_function | IMP dehydrogenase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006164 | biological_process | purine nucleotide biosynthetic process |
| C | 0006177 | biological_process | GMP biosynthetic process |
| C | 0006183 | biological_process | GTP biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0003938 | molecular_function | IMP dehydrogenase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006164 | biological_process | purine nucleotide biosynthetic process |
| D | 0006177 | biological_process | GMP biosynthetic process |
| D | 0006183 | biological_process | GTP biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
| site_id | PS00487 |
| Number of Residues | 13 |
| Details | IMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. IKVGIGpGSICtT |
| Chain | Residue | Details |
| A | ILE209-THR221 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Thioimidate intermediate => ECO:0000250|UniProtKB:P50097 |
| Chain | Residue | Details |
| A | CYS219 | |
| B | CYS219 | |
| C | CYS219 | |
| D | CYS219 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P9WKI7 |
| Chain | Residue | Details |
| A | ARG315 | |
| B | ARG315 | |
| C | ARG315 | |
| D | ARG315 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P50097 |
| Chain | Residue | Details |
| A | HIS385 | |
| B | ASP163 | |
| B | GLY212 | |
| B | GLU383 | |
| B | SER384 | |
| B | HIS385 | |
| C | ASP163 | |
| C | GLY212 | |
| C | GLU383 | |
| C | SER384 | |
| C | HIS385 | |
| D | ASP163 | |
| D | GLY212 | |
| D | GLU383 | |
| D | SER384 | |
| D | HIS385 | |
| A | ASP163 | |
| A | GLY212 | |
| A | GLU383 | |
| A | SER384 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: in other chain => ECO:0000250|UniProtKB:P50097 |
| Chain | Residue | Details |
| A | GLY214 | |
| A | GLY216 | |
| A | CYS219 | |
| B | GLY214 | |
| B | GLY216 | |
| B | CYS219 | |
| C | GLY214 | |
| C | GLY216 | |
| C | CYS219 | |
| D | GLY214 | |
| D | GLY216 | |
| D | CYS219 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23668331 |
| Chain | Residue | Details |
| C | GLY275 | |
| C | TYR299 | |
| C | GLU329 | |
| D | SER217 | |
| D | ASP252 | |
| D | GLY275 | |
| D | TYR299 | |
| D | GLU329 | |
| A | SER217 | |
| A | ASP252 | |
| A | GLY275 | |
| A | TYR299 | |
| A | GLU329 | |
| B | SER217 | |
| B | ASP252 | |
| B | GLY275 | |
| B | TYR299 | |
| B | GLU329 | |
| C | SER217 | |
| C | ASP252 |
