4BV2
CRYSTAL STRUCTURE OF SIR2 IN COMPLEX WITH THE INHIBITOR EX-527, 2'-O-ACETYL-ADP-RIBOSE AND DEACETYLATED P53-PEPTIDE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006338 | biological_process | chromatin remodeling |
| A | 0006476 | biological_process | protein deacetylation |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016740 | molecular_function | transferase activity |
| A | 0017136 | molecular_function | NAD-dependent histone deacetylase activity |
| A | 0034979 | molecular_function | NAD-dependent protein lysine deacetylase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051287 | molecular_function | NAD binding |
| A | 0070403 | molecular_function | NAD+ binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006338 | biological_process | chromatin remodeling |
| B | 0006476 | biological_process | protein deacetylation |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016740 | molecular_function | transferase activity |
| B | 0017136 | molecular_function | NAD-dependent histone deacetylase activity |
| B | 0034979 | molecular_function | NAD-dependent protein lysine deacetylase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051287 | molecular_function | NAD binding |
| B | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 1246 |
| Chain | Residue |
| A | CYS124 |
| A | CYS127 |
| A | LYS129 |
| A | CYS148 |
| A | CYS151 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE OCZ A 1247 |
| Chain | Residue |
| A | ASN99 |
| A | ILE100 |
| A | ILE159 |
| A | OAD1248 |
| A | SER25 |
| A | ILE30 |
| A | PRO31 |
| A | PHE33 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE OAD A 1248 |
| Chain | Residue |
| A | GLY21 |
| A | ALA22 |
| A | GLY23 |
| A | THR26 |
| A | PRO27 |
| A | ASP32 |
| A | PHE33 |
| A | GLN98 |
| A | HIS116 |
| A | PHE162 |
| A | GLY188 |
| A | SER189 |
| A | SER190 |
| A | VAL193 |
| A | ASN214 |
| A | LEU215 |
| A | MET230 |
| A | ASP231 |
| A | VAL232 |
| A | OCZ1247 |
| E | LYS3 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE OCZ B 1247 |
| Chain | Residue |
| B | SER25 |
| B | ILE30 |
| B | PRO31 |
| B | PHE33 |
| B | MET71 |
| B | GLN98 |
| B | ASN99 |
| B | ILE100 |
| B | ASP101 |
| B | ILE159 |
| B | OAD1248 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE OAD B 1248 |
| Chain | Residue |
| B | GLY21 |
| B | ALA22 |
| B | GLY23 |
| B | THR26 |
| B | PRO27 |
| B | ASP32 |
| B | PHE33 |
| B | PHE48 |
| B | GLN98 |
| B | HIS116 |
| B | VAL160 |
| B | PHE162 |
| B | SER189 |
| B | SER190 |
| B | VAL193 |
| B | ASN214 |
| B | LEU215 |
| B | MET230 |
| B | ASP231 |
| B | VAL232 |
| B | OCZ1247 |
| H | LYS3 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 1249 |
| Chain | Residue |
| B | CYS124 |
| B | CYS127 |
| B | LYS129 |
| B | CYS148 |
| B | CYS151 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:29474172, ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| E | LYS2 | |
| H | LYS2 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-methyllysine; by KMT5A; alternate => ECO:0000269|PubMed:17707234, ECO:0000269|PubMed:20870725, ECO:0000269|PubMed:22864287 |
| Chain | Residue | Details |
| E | LYS3 | |
| A | GLY216 | |
| A | ASP231 | |
| A | VAL232 | |
| B | ALA22 | |
| B | THR26 | |
| B | ARG34 | |
| B | GLN98 | |
| B | HIS116 | |
| B | SER189 | |
| B | SER190 | |
| H | LYS3 | |
| B | ASN214 | |
| B | LEU215 | |
| B | GLY216 | |
| B | ASP231 | |
| B | VAL232 | |
| A | ARG34 | |
| A | GLN98 | |
| A | HIS116 | |
| A | SER189 | |
| A | SER190 | |
| A | ASN214 | |
| A | LEU215 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:11124955, ECO:0000269|PubMed:22214662, ECO:0000269|Ref.37 |
| Chain | Residue | Details |
| E | LYS7 | |
| A | ILE100 | |
| H | LYS7 | |
| B | PHE33 | |
| B | ILE100 | |
| B | ASP101 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15780941, ECO:0000269|PubMed:16768447, ECO:0000269|PubMed:16905097, ECO:0000269|PubMed:18786399, ECO:0000269|PubMed:19801667, ECO:0000269|PubMed:21080423, ECO:0007744|PDB:1YC5, ECO:0007744|PDB:2H2D, ECO:0007744|PDB:2H4F, ECO:0007744|PDB:3D4B, ECO:0007744|PDB:3JR3, ECO:0007744|PDB:3PDH |
| Chain | Residue | Details |
| A | CYS124 | |
| A | CYS127 | |
| A | CYS148 | |
| A | CYS151 | |
| B | CYS124 | |
| B | CYS127 | |
| B | CYS148 | |
| B | CYS151 |
