6RNH
Structure of C-terminal truncated Plasmodium falciparum IMP-nucleotidase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| 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 | 0008253 | molecular_function | 5'-nucleotidase activity |
| A | 0009117 | biological_process | nucleotide metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071590 | biological_process | nicotinamide riboside biosynthetic process |
| A | 0071592 | biological_process | nicotinic acid riboside biosynthetic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006190 | biological_process | inosine salvage |
| B | 0006204 | biological_process | IMP catabolic process |
| B | 0008253 | molecular_function | 5'-nucleotidase activity |
| B | 0009117 | biological_process | nucleotide metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071590 | biological_process | nicotinamide riboside biosynthetic process |
| B | 0071592 | biological_process | nicotinic acid riboside biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 501 |
| Chain | Residue |
| A | CYS356 |
| A | LYS371 |
| A | HIS398 |
| A | PHE403 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 501 |
| Chain | Residue |
| A | ASP184 |
| A | VAL186 |
| B | LEU319 |
| B | ASN320 |
| B | GLU324 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:32591529 |
| Chain | Residue | Details |
| A | ASP170 | |
| B | ASP170 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:32591529 |
| Chain | Residue | Details |
| A | ASP172 | |
| B | ASP172 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:32591529, ECO:0007744|PDB:6RMD |
| Chain | Residue | Details |
| A | LYS132 | |
| A | HIS150 | |
| B | LYS132 | |
| B | HIS150 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:32591529, ECO:0007744|PDB:6RME, ECO:0007744|PDB:6RMW |
| Chain | Residue | Details |
| A | ASP170 | |
| B | ASP170 | |
| B | ASP172 | |
| B | ASP178 | |
| B | THR204 | |
| B | SER207 | |
| B | SER308 | |
| B | ASP363 | |
| B | LYS371 | |
| B | ASP394 | |
| A | ASP172 | |
| A | ASP178 | |
| A | THR204 | |
| A | SER207 | |
| A | SER308 | |
| A | ASP363 | |
| A | LYS371 | |
| A | ASP394 |
