8CCZ
Crystal structure of human Sirt3 in complex with an inhibiting HIV1 Tat-37-59 peptide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0017136 | molecular_function | histone deacetylase activity, NAD-dependent |
| A | 0051287 | molecular_function | NAD binding |
| A | 0070403 | molecular_function | NAD+ binding |
| B | 0017136 | molecular_function | histone deacetylase activity, NAD-dependent |
| B | 0051287 | molecular_function | NAD binding |
| B | 0070403 | molecular_function | NAD+ binding |
| C | 0001070 | molecular_function | RNA-binding transcription regulator activity |
| C | 0042025 | cellular_component | host cell nucleus |
| C | 0050434 | biological_process | positive regulation of viral transcription |
| D | 0001070 | molecular_function | RNA-binding transcription regulator activity |
| D | 0042025 | cellular_component | host cell nucleus |
| D | 0050434 | biological_process | positive regulation of viral transcription |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00236","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12186850","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16788062","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18794531","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36896611","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 54 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23897466","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19535340","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23897466","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36896611","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37720100","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19535340","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23897466","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36896611","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8R104","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 16 |
| Details | Motif: {"description":"Nuclear localization signal, RNA-binding (TAR), and protein transduction","evidences":[{"source":"HAMAP-Rule","id":"MF_04079","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine; by host EP300 and GCN5L2","evidences":[{"source":"HAMAP-Rule","id":"MF_04079","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Asymmetric dimethylarginine; by host PRMT6","evidences":[{"source":"HAMAP-Rule","id":"MF_04079","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
