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 | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"32591529","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"32591529","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"32591529","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6RMD","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 18 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"32591529","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6RME","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6RMW","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |