4TWJ
The structure of Sir2Af2 bound to a myristoylated histone peptide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006338 | biological_process | chromatin remodeling |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016740 | molecular_function | transferase activity |
| A | 0017136 | molecular_function | histone deacetylase activity, NAD-dependent |
| A | 0034979 | molecular_function | NAD-dependent protein lysine deacetylase activity |
| A | 0036054 | molecular_function | protein-malonyllysine demalonylase activity |
| A | 0036055 | molecular_function | protein-succinyllysine desuccinylase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051287 | molecular_function | NAD binding |
| A | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| A | CYS126 |
| A | CYS129 |
| A | CYS150 |
| A | CYS153 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue ACT A 302 |
| Chain | Residue |
| A | ASN59 |
| A | PRO60 |
| A | ARG61 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 303 |
| Chain | Residue |
| A | ASP103 |
| A | HOH533 |
| A | ASN101 |
| A | ILE102 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 304 |
| Chain | Residue |
| A | ALA24 |
| A | SER193 |
| A | HOH487 |
| A | HOH579 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue ACT A 305 |
| Chain | Residue |
| A | GLY25 |
| A | PHE75 |
| A | LYS234 |
| A | ALA235 |
| A | GLY236 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue ACT A 306 |
| Chain | Residue |
| A | LYS95 |
| A | GLU176 |
| A | GLU180 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 307 |
| Chain | Residue |
| A | GLU137 |
| A | PHE138 |
| A | ARG149 |
| A | ARG151 |
| A | HOH451 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 101 |
| Chain | Residue |
| A | TYR197 |
| A | HOH402 |
| B | ARG6 |
| B | ARG8 |
| B | HOH201 |
| B | HOH203 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00236","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01121","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15023335","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15780941","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"22343720","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"11080160","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15150415","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17289592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19113941","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
