3CM6
Crystal structure of cell-death related nuclease 4 (CRN-4) bound with Er
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000175 | molecular_function | 3'-5'-RNA exonuclease activity |
| A | 0000467 | biological_process | exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0003697 | molecular_function | single-stranded DNA binding |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0004520 | molecular_function | DNA endonuclease activity |
| A | 0004527 | molecular_function | exonuclease activity |
| A | 0004536 | molecular_function | DNA nuclease activity |
| A | 0004540 | molecular_function | RNA nuclease activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006308 | biological_process | DNA catabolic process |
| A | 0006309 | biological_process | apoptotic DNA fragmentation |
| A | 0006401 | biological_process | RNA catabolic process |
| A | 0006915 | biological_process | apoptotic process |
| A | 0008408 | molecular_function | 3'-5' exonuclease activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000175 | molecular_function | 3'-5'-RNA exonuclease activity |
| B | 0000467 | biological_process | exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0003697 | molecular_function | single-stranded DNA binding |
| B | 0004518 | molecular_function | nuclease activity |
| B | 0004520 | molecular_function | DNA endonuclease activity |
| B | 0004527 | molecular_function | exonuclease activity |
| B | 0004536 | molecular_function | DNA nuclease activity |
| B | 0004540 | molecular_function | RNA nuclease activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006308 | biological_process | DNA catabolic process |
| B | 0006309 | biological_process | apoptotic DNA fragmentation |
| B | 0006401 | biological_process | RNA catabolic process |
| B | 0006915 | biological_process | apoptotic process |
| B | 0008408 | molecular_function | 3'-5' exonuclease activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 299 |
| Chain | Residue |
| A | CYS210 |
| A | CYS260 |
| A | CYS263 |
| A | CYS270 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ER3 A 300 |
| Chain | Residue |
| A | ASP15 |
| A | PHE16 |
| A | GLU17 |
| A | ASP184 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 299 |
| Chain | Residue |
| B | CYS260 |
| B | CYS263 |
| B | CYS270 |
| B | CYS210 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ER3 B 300 |
| Chain | Residue |
| B | ASP15 |
| B | GLU17 |
| B | ASP184 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 360 |
| Details | Domain: {"description":"Exonuclease","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27529560","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5DK5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18981218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27529560","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CG7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CM5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CM6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5DK5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
