3SAG
Crystal structure of the human RRP6 catalytic domain with D313N mutation in the active site
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
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 | 0006139 | biological_process | nucleobase-containing compound metabolic process |
A | 0008408 | molecular_function | 3'-5' exonuclease activity |
A | 0044237 | biological_process | cellular metabolic process |
B | 0000166 | molecular_function | nucleotide 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 | 0006139 | biological_process | nucleobase-containing compound metabolic process |
B | 0008408 | molecular_function | 3'-5' exonuclease activity |
B | 0044237 | biological_process | cellular metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE YT3 A 1 |
Chain | Residue |
A | HOH73 |
A | HOH104 |
A | HOH116 |
A | GLU296 |
A | GLU299 |
A | ASP488 |
A | GLU489 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE YT3 A 3 |
Chain | Residue |
A | ASP440 |
A | HOH630 |
A | HOH632 |
A | HOH28 |
A | ASP404 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 1 |
Chain | Residue |
B | HOH33 |
B | HOH38 |
B | HOH40 |
B | ASN313 |
B | ASP371 |
B | HOH611 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE YT3 B 2 |
Chain | Residue |
B | HOH43 |
B | HOH128 |
B | GLU296 |
B | GLU299 |
B | ASP488 |
B | GLU489 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21705430, ECO:0007744|PDB:3SAH |
Chain | Residue | Details |
A | ASP440 | |
A | GLU315 | |
B | ASN313 | |
B | GLU315 | |
B | ASP440 | |
A | ASN313 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21705430, ECO:0007744|PDB:3SAF, ECO:0007744|PDB:3SAG, ECO:0007744|PDB:3SAH |
Chain | Residue | Details |
A | ASP371 | |
B | ASP371 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Not ubiquitinated => ECO:0000269|PubMed:36912080 |
Chain | Residue | Details |
A | LYS583 | |
B | LYS583 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000269|PubMed:36912080, ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
A | LYS583 | |
B | LYS583 |