4QOZ
Crystal structure of the histone mRNA stem-loop, stem-loop binding protein (phosphorylated), and 3'hExo ternary complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0000175 | molecular_function | 3'-5'-RNA exonuclease activity |
| B | 0003676 | molecular_function | nucleic acid binding |
| C | 0003723 | molecular_function | RNA binding |
| C | 0003729 | molecular_function | mRNA binding |
| E | 0000175 | molecular_function | 3'-5'-RNA exonuclease activity |
| E | 0003676 | molecular_function | nucleic acid binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 68 |
| Details | Domain: {"description":"SAP","evidences":[{"source":"PROSITE-ProRule","id":"PRU00186","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"15451662","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1W0H","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15451662","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1W0H","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"22439849","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 784 |
| Chain | Residue | Details |
| B | ASP134 | metal ligand |
| B | GLU136 | electrostatic stabiliser, metal ligand, proton acceptor |
| B | ASP234 | metal ligand |
| B | HIS293 | electrostatic stabiliser, proton acceptor |
| B | ASP298 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 784 |
| Chain | Residue | Details |
| E | ASP134 | metal ligand |
| E | GLU136 | electrostatic stabiliser, metal ligand, proton acceptor |
| E | ASP234 | metal ligand |
| E | HIS293 | electrostatic stabiliser, proton acceptor |
| E | ASP298 | metal ligand |
