5DK5
Crystal structure of CRN-4-MES complex
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 | 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 | 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 | 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 | 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 301 |
Chain | Residue |
A | CYS210 |
A | CYS260 |
A | CYS263 |
A | CYS270 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue MES A 302 |
Chain | Residue |
A | ASP180 |
A | ASP184 |
A | HOH479 |
A | GLU17 |
A | PHE71 |
A | THR72 |
A | THR161 |
A | HIS179 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue MG A 303 |
Chain | Residue |
A | ASP15 |
A | GLU17 |
A | ASP184 |
A | HOH405 |
A | HOH479 |
A | HOH566 |
A | HOH570 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue IPA A 304 |
Chain | Residue |
A | ALA159 |
A | THR160 |
A | THR161 |
A | HOH659 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue IPA A 305 |
Chain | Residue |
A | TRP214 |
A | HOH574 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue IPA A 306 |
Chain | Residue |
A | ARG215 |
A | GLN276 |
A | ASP280 |
A | HOH431 |
A | HOH679 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue ZN B 301 |
Chain | Residue |
B | CYS210 |
B | CYS260 |
B | CYS263 |
B | CYS270 |
site_id | AC8 |
Number of Residues | 9 |
Details | binding site for residue MES B 302 |
Chain | Residue |
B | GLU17 |
B | THR72 |
B | THR161 |
B | HIS179 |
B | ASP180 |
B | ASP184 |
B | HOH410 |
B | HOH426 |
B | HOH431 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue MG B 303 |
Chain | Residue |
B | ASP15 |
B | GLU17 |
B | ASP184 |
B | HOH401 |
B | HOH426 |
B | HOH505 |
B | HOH534 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue IPA B 304 |
Chain | Residue |
B | SER112 |
B | ARG113 |
B | ASN140 |
B | TYR142 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue IPA B 305 |
Chain | Residue |
B | TYR27 |
B | ARG118 |
B | TYR122 |
B | PHE236 |
B | PHE291 |
B | HOH473 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue IPA B 306 |
Chain | Residue |
B | ARG215 |
B | ARG216 |
B | ASP280 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue IPA B 307 |
Chain | Residue |
B | ASP111 |
B | ASN162 |
B | HOH431 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27529560, ECO:0007744|PDB:5DK5 |
Chain | Residue | Details |
A | ASP15 | |
A | GLU17 | |
A | ASP184 | |
B | ASP15 | |
B | GLU17 | |
B | ASP184 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18981218, ECO:0000269|PubMed:27529560, ECO:0007744|PDB:3CG7, ECO:0007744|PDB:3CM5, ECO:0007744|PDB:3CM6, ECO:0007744|PDB:5DK5 |
Chain | Residue | Details |
A | CYS210 | |
A | CYS260 | |
A | CYS263 | |
A | CYS270 | |
B | CYS210 | |
B | CYS260 | |
B | CYS263 | |
B | CYS270 |