1M2N
Sir2 homologues (D102G/F159A/R170A) mutant-2'-O-acetyl ADP ribose complex
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 | 0070403 | molecular_function | NAD+ binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006338 | biological_process | chromatin remodeling |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016740 | molecular_function | transferase activity |
B | 0017136 | molecular_function | histone deacetylase activity, NAD-dependent |
B | 0034979 | molecular_function | NAD-dependent protein lysine deacetylase activity |
B | 0036054 | molecular_function | protein-malonyllysine demalonylase activity |
B | 0036055 | molecular_function | protein-succinyllysine desuccinylase activity |
B | 0046872 | molecular_function | metal ion 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 999 |
Chain | Residue |
A | CYS124 |
A | CYS127 |
A | CYS145 |
A | CYS148 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 999 |
Chain | Residue |
B | CYS124 |
B | CYS127 |
B | CYS145 |
B | CYS148 |
B | SER150 |
site_id | AC3 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE OAD B 1001 |
Chain | Residue |
A | GLY20 |
A | ALA21 |
A | GLY22 |
A | GLU26 |
A | THR31 |
A | PHE32 |
A | ARG33 |
A | GLN98 |
A | HIS116 |
A | VAL157 |
A | GLY185 |
A | THR186 |
A | SER187 |
A | VAL190 |
A | ASN211 |
A | PRO212 |
A | LYS228 |
A | ALA229 |
A | LYS247 |
B | HOH2002 |
B | HOH2087 |
site_id | AC4 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE OAD B 2001 |
Chain | Residue |
B | GLY20 |
B | ALA21 |
B | GLY22 |
B | GLU26 |
B | THR31 |
B | PHE32 |
B | ARG33 |
B | GLN98 |
B | HIS116 |
B | VAL157 |
B | GLY185 |
B | THR186 |
B | SER187 |
B | VAL190 |
B | ASN211 |
B | PRO212 |
B | ASP213 |
B | LYS228 |
B | ALA229 |
B | LYS247 |
B | HOH2003 |
B | HOH2027 |
B | HOH2076 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 484 |
Details | Domain: {"description":"Deacetylase sirtuin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00236","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00236","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 54 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01121","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11336676","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01121","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01121","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11336676","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12091395","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |