4NV0
Crystal structure of cytosolic 5'-nucleotidase IIIB (cN-IIIB) bound to 7-methylguanosine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0008252 | molecular_function | nucleotidase activity |
A | 0008253 | molecular_function | 5'-nucleotidase activity |
A | 0009117 | biological_process | nucleotide metabolic process |
A | 0009158 | biological_process | ribonucleoside monophosphate catabolic process |
A | 0016311 | biological_process | dephosphorylation |
A | 0016787 | molecular_function | hydrolase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0106411 | molecular_function | XMP 5'-nucleosidase activity |
A | 1901069 | biological_process | guanosine-containing compound catabolic process |
B | 0000166 | molecular_function | nucleotide binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0008252 | molecular_function | nucleotidase activity |
B | 0008253 | molecular_function | 5'-nucleotidase activity |
B | 0009117 | biological_process | nucleotide metabolic process |
B | 0009158 | biological_process | ribonucleoside monophosphate catabolic process |
B | 0016311 | biological_process | dephosphorylation |
B | 0016787 | molecular_function | hydrolase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0106411 | molecular_function | XMP 5'-nucleosidase activity |
B | 1901069 | biological_process | guanosine-containing compound catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PGE A 401 |
Chain | Residue |
A | ARG13 |
B | HOH695 |
A | ALA33 |
A | GLU36 |
A | ARG37 |
A | ASN40 |
A | ILE44 |
A | HOH723 |
A | HOH768 |
B | GLU155 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 402 |
Chain | Residue |
A | ASP55 |
A | ASP57 |
A | ASP245 |
A | MGF404 |
A | HOH626 |
A | HOH627 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE MG7 A 403 |
Chain | Residue |
A | ASP57 |
A | PHE75 |
A | ARG100 |
A | GLU103 |
A | TRP120 |
A | TRP121 |
A | SER124 |
A | GLY173 |
A | HOH515 |
A | HOH540 |
A | HOH579 |
A | HOH586 |
A | HOH605 |
A | HOH662 |
A | HOH776 |
site_id | AC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE MGF A 404 |
Chain | Residue |
A | ASP55 |
A | PHE56 |
A | ASP57 |
A | SER171 |
A | ALA172 |
A | LYS219 |
A | MG402 |
A | HOH523 |
A | HOH540 |
A | HOH626 |
A | HOH627 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 401 |
Chain | Residue |
B | ASP55 |
B | ASP57 |
B | ASP245 |
B | MGF403 |
B | HOH644 |
B | HOH645 |
site_id | AC6 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE MG7 B 402 |
Chain | Residue |
B | SER73 |
B | PHE75 |
B | ASN79 |
B | TYR96 |
B | GLU103 |
B | TRP120 |
B | TRP121 |
B | SER124 |
B | HOH502 |
B | HOH521 |
B | HOH554 |
B | HOH574 |
B | HOH639 |
B | HOH663 |
B | HOH693 |
B | HOH719 |
site_id | AC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE MGF B 403 |
Chain | Residue |
B | ASP55 |
B | PHE56 |
B | ASP57 |
B | SER171 |
B | ALA172 |
B | LYS219 |
B | MG401 |
B | HOH502 |
B | HOH506 |
B | HOH644 |
B | HOH645 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:24603684 |
Chain | Residue | Details |
A | ASP55 | |
B | ASP55 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:24603684 |
Chain | Residue | Details |
A | ASP57 | |
B | ASP57 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24603684 |
Chain | Residue | Details |
A | ASP245 | |
B | ASP55 | |
B | ASP57 | |
B | GLU103 | |
B | SER124 | |
B | ASP245 | |
A | ASP55 | |
A | ASP57 | |
A | GLU103 | |
A | SER124 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9H0P0 |
Chain | Residue | Details |
A | SER171 | |
B | SER171 |