1J8F
HUMAN SIRT2 HISTONE DEACETYLASE
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 |
| C | 0017136 | molecular_function | NAD-dependent histone deacetylase activity |
| C | 0051287 | molecular_function | NAD binding |
| C | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1001 |
| Chain | Residue |
| A | CYS195 |
| A | CYS200 |
| A | CYS221 |
| A | CYS224 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 2001 |
| Chain | Residue |
| B | CYS195 |
| B | SER197 |
| B | CYS200 |
| B | CYS221 |
| B | CYS224 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 3001 |
| Chain | Residue |
| C | CYS195 |
| C | CYS200 |
| C | CYS221 |
| C | CYS224 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00236 |
| Chain | Residue | Details |
| A | HIS187 | |
| B | HIS187 | |
| C | HIS187 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25672491, ECO:0007744|PDB:4RMG |
| Chain | Residue | Details |
| A | ALA85 | |
| B | THR262 | |
| B | ASN286 | |
| B | CYS324 | |
| C | ALA85 | |
| C | ASP95 | |
| C | GLN167 | |
| C | THR262 | |
| C | ASN286 | |
| C | CYS324 | |
| A | ASP95 | |
| A | GLN167 | |
| A | THR262 | |
| A | ASN286 | |
| A | CYS324 | |
| B | ALA85 | |
| B | ASP95 | |
| B | GLN167 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| 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 | |
| C | CYS200 | |
| C | CYS221 | |
| C | CYS224 | |
| A | CYS200 | |
| A | CYS221 | |
| A | CYS224 | |
| B | CYS195 | |
| B | CYS200 | |
| B | CYS221 | |
| B | CYS224 | |
| C | CYS195 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 9 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q5RJQ4 |
| Chain | Residue | Details |
| A | SER53 | |
| A | SER100 | |
| A | SER207 | |
| B | SER53 | |
| B | SER100 | |
| B | SER207 | |
| C | SER53 | |
| C | SER100 | |
| C | SER207 |
