4NWI
Crystal structure of cytosolic 5'-nucleotidase IIIB (cN-IIIB) bound to cytidine
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 | 6 |
Details | BINDING SITE FOR RESIDUE MG A 401 |
Chain | Residue |
A | ASP55 |
A | ASP57 |
A | ASP245 |
A | HOH628 |
A | HOH629 |
A | HOH630 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE CTN A 402 |
Chain | Residue |
A | GLU103 |
A | TRP120 |
A | TRP121 |
A | SER124 |
A | ALA172 |
A | GLY173 |
A | THR216 |
A | HOH557 |
A | ASP57 |
A | PHE75 |
A | ARG100 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 403 |
Chain | Residue |
A | ASP55 |
A | ALA172 |
A | LYS219 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 401 |
Chain | Residue |
B | ASP55 |
B | ASP57 |
B | ASP245 |
B | HOH636 |
B | HOH637 |
B | HOH638 |
site_id | AC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE CTN B 402 |
Chain | Residue |
B | ASP57 |
B | PHE75 |
B | TYR96 |
B | GLU103 |
B | TRP120 |
B | TRP121 |
B | SER124 |
B | GLY173 |
B | THR216 |
B | HOH553 |
B | HOH561 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL B 403 |
Chain | Residue |
B | ASP55 |
B | ALA172 |
B | LYS219 |
B | HOH501 |
B | HOH636 |
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 | ASP55 | |
B | ASP245 | |
A | ASP57 | |
A | GLU103 | |
A | SER124 | |
A | ASP245 | |
B | ASP55 | |
B | ASP57 | |
B | GLU103 | |
B | SER124 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9H0P0 |
Chain | Residue | Details |
A | SER171 | |
B | SER171 |