5MJ7
Structure of the C. elegans nucleoside hydrolase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0006152 | biological_process | purine nucleoside catabolic process |
| A | 0008477 | molecular_function | purine nucleosidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
| A | 0045437 | molecular_function | uridine nucleosidase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047622 | molecular_function | adenosine nucleosidase activity |
| A | 0047724 | molecular_function | inosine nucleosidase activity |
| A | 0050263 | molecular_function | ribosylpyrimidine nucleosidase activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0006152 | biological_process | purine nucleoside catabolic process |
| B | 0008477 | molecular_function | purine nucleosidase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
| B | 0045437 | molecular_function | uridine nucleosidase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047622 | molecular_function | adenosine nucleosidase activity |
| B | 0047724 | molecular_function | inosine nucleosidase activity |
| B | 0050263 | molecular_function | ribosylpyrimidine nucleosidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 401 |
| Chain | Residue |
| A | ASP13 |
| A | ASP18 |
| A | ILE133 |
| A | ASP254 |
| A | TRS402 |
| A | HOH522 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue TRS A 402 |
| Chain | Residue |
| A | ILE133 |
| A | ASN178 |
| A | CYS253 |
| A | ASP254 |
| A | CA401 |
| A | HOH522 |
| A | HOH525 |
| A | HOH601 |
| A | HOH659 |
| A | VAL15 |
| A | ASP17 |
| A | ASP18 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 401 |
| Chain | Residue |
| B | ASP13 |
| B | ASP18 |
| B | ILE133 |
| B | ASP254 |
| B | TRS402 |
| B | HOH520 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue TRS B 402 |
| Chain | Residue |
| B | VAL15 |
| B | ASP17 |
| B | ASP18 |
| B | ILE133 |
| B | ASN178 |
| B | CYS253 |
| B | ASP254 |
| B | CA401 |
| B | HOH504 |
| B | HOH520 |
| B | HOH525 |
| B | HOH630 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"28218438","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5MJ7","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28218438","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5MJ7","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
