6QCN
Human Sirt2 in complex with ADP-ribose and the inhibitor quercetin
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0017136 | molecular_function | NAD-dependent histone deacetylase activity |
A | 0051287 | molecular_function | NAD binding |
A | 0070403 | molecular_function | NAD+ binding |
B | 0017136 | molecular_function | NAD-dependent histone deacetylase activity |
B | 0051287 | molecular_function | NAD binding |
B | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue ZN A 401 |
Chain | Residue |
A | CYS195 |
A | CYS200 |
A | CYS221 |
A | CYS224 |
site_id | AC2 |
Number of Residues | 19 |
Details | binding site for residue AR6 A 402 |
Chain | Residue |
A | PHE96 |
A | ARG97 |
A | TYR104 |
A | GLN167 |
A | HIS187 |
A | GLY261 |
A | THR262 |
A | SER263 |
A | ASN286 |
A | LYS287 |
A | GLU288 |
A | GLY322 |
A | GLU323 |
A | CYS324 |
A | GLY84 |
A | ALA85 |
A | GLY86 |
A | THR89 |
A | ASP95 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue QUE A 403 |
Chain | Residue |
A | TYR114 |
A | GLU120 |
A | HOH507 |
B | GLU120 |
B | PHE235 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue ZN B 401 |
Chain | Residue |
B | CYS195 |
B | CYS200 |
B | CYS221 |
B | CYS224 |
site_id | AC5 |
Number of Residues | 22 |
Details | binding site for residue AR6 B 402 |
Chain | Residue |
B | GLY84 |
B | ALA85 |
B | GLY86 |
B | THR89 |
B | ASP95 |
B | PHE96 |
B | ARG97 |
B | TYR104 |
B | GLN167 |
B | HIS187 |
B | PHE235 |
B | GLY261 |
B | THR262 |
B | SER263 |
B | VAL266 |
B | ASN286 |
B | LYS287 |
B | GLU288 |
B | GLU323 |
B | CYS324 |
B | HOH501 |
B | HOH506 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00236 |
Chain | Residue | Details |
A | HIS187 | |
B | HIS187 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25672491, ECO:0007744|PDB:4RMG |
Chain | Residue | Details |
A | GLN167 | |
A | THR262 | |
A | ASN286 | |
A | CYS324 | |
B | ALA85 | |
B | ASP95 | |
B | GLN167 | |
B | THR262 | |
B | ASN286 | |
B | CYS324 | |
A | ALA85 | |
A | ASP95 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:11427894, ECO:0000269|PubMed:23454361, ECO:0000269|PubMed:24389023, ECO:0000269|PubMed:25672491, ECO:0000269|PubMed:25704306, ECO:0007744|PDB:4R8M |
Chain | Residue | Details |
A | CYS195 | |
A | CYS200 | |
A | CYS221 | |
A | CYS224 | |
B | CYS195 | |
B | CYS200 | |
B | CYS221 | |
B | CYS224 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q5RJQ4 |
Chain | Residue | Details |
B | SER100 | |
B | SER207 | |
A | SER100 | |
A | SER207 |