2HBL
Structure of the yeast nuclear exosome component, Rrp6p, reveals an interplay between the active site and the HRDC domain; Protein in complex with Mn, Zn, and AMP
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 1001 |
| Chain | Residue |
| A | ASP238 |
| A | GLU240 |
| A | ASP365 |
| A | AMP2001 |
| A | HOH2002 |
| A | HOH2003 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 1002 |
| Chain | Residue |
| A | HOH2004 |
| A | HOH2005 |
| A | HOH2006 |
| A | ASP238 |
| A | ASP296 |
| A | AMP2001 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE AMP A 2001 |
| Chain | Residue |
| A | ASP238 |
| A | LEU239 |
| A | GLU240 |
| A | HIS241 |
| A | TRP299 |
| A | LYS342 |
| A | GLN345 |
| A | TRP349 |
| A | ZN1001 |
| A | MN1002 |
| A | HOH2004 |
| A | HOH2126 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 166 |
| Details | Domain: {"description":"3'-5' exonuclease","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 80 |
| Details | Domain: {"description":"HRDC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00328","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16882719","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2HBL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HBM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16882719","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2HBM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16882719","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2HBK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HBL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HBM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
