6RMD
Structure of ATP bound Plasmodium falciparum IMP-nucleotidase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006190 | biological_process | inosine salvage |
| A | 0006204 | biological_process | IMP catabolic process |
| A | 0009117 | biological_process | nucleotide metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050483 | molecular_function | IMP 5'-nucleotidase activity |
| A | 0071590 | biological_process | nicotinamide riboside biosynthetic process |
| A | 0071592 | biological_process | nicotinic acid riboside biosynthetic process |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0006190 | biological_process | inosine salvage |
| D | 0009117 | biological_process | nucleotide metabolic process |
| D | 0050483 | molecular_function | IMP 5'-nucleotidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 501 |
| Chain | Residue |
| A | GLU173 |
| A | GLU245 |
| A | PHE358 |
| A | LYS371 |
| A | LEU397 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue ATP D 501 |
| Chain | Residue |
| D | LEU154 |
| D | GLN418 |
| D | GLU419 |
| D | ALA422 |
| D | CYS423 |
| D | LYS132 |
| D | TYR133 |
| D | HIS150 |
| D | ASN153 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue EDO D 502 |
| Chain | Residue |
| D | ARG71 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:32591529 |
| Chain | Residue | Details |
| D | ASP170 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:32591529 |
| Chain | Residue | Details |
| D | ASP172 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:32591529, ECO:0007744|PDB:6RMD |
| Chain | Residue | Details |
| D | LYS132 | |
| D | HIS150 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 9 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:32591529, ECO:0007744|PDB:6RME, ECO:0007744|PDB:6RMW |
| Chain | Residue | Details |
| D | ASP170 | |
| D | ASP172 | |
| D | ASP178 | |
| D | THR204 | |
| D | SER207 | |
| D | SER308 | |
| D | ASP363 | |
| D | LYS371 | |
| D | ASP394 |
