1ICI
CRYSTAL STRUCTURE OF A SIR2 HOMOLOG-NAD COMPLEX
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006338 | biological_process | chromatin remodeling |
| A | 0006351 | biological_process | DNA-templated transcription |
| 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 | 0006351 | biological_process | DNA-templated transcription |
| 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 2001 |
| Chain | Residue |
| A | CYS124 |
| A | CYS127 |
| A | CYS145 |
| A | CYS148 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 2002 |
| Chain | Residue |
| B | CYS124 |
| B | CYS127 |
| B | CYS145 |
| B | CYS148 |
| site_id | AC3 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD A 1001 |
| Chain | Residue |
| A | ALA21 |
| A | GLY22 |
| A | GLU26 |
| A | PHE32 |
| A | PRO44 |
| A | GLN98 |
| A | HIS116 |
| A | GLY185 |
| A | THR186 |
| A | SER187 |
| A | VAL190 |
| A | ASN211 |
| A | PRO212 |
| A | ASP213 |
| A | LYS228 |
| A | ALA229 |
| A | HOH2018 |
| A | HOH2029 |
| A | HOH2030 |
| A | HOH2032 |
| A | HOH2038 |
| A | HOH2054 |
| A | HOH2055 |
| A | HOH2057 |
| A | HOH2086 |
| A | HOH2097 |
| A | HOH2117 |
| A | GLY20 |
| site_id | AC4 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD B 1002 |
| Chain | Residue |
| B | GLY20 |
| B | ALA21 |
| B | GLY22 |
| B | GLU26 |
| B | PHE32 |
| B | PRO44 |
| B | GLN98 |
| B | HIS116 |
| B | GLY185 |
| B | THR186 |
| B | SER187 |
| B | VAL190 |
| B | ASN211 |
| B | PRO212 |
| B | ASP213 |
| B | LYS228 |
| B | ALA229 |
| B | HOH2011 |
| B | HOH2016 |
| B | HOH2023 |
| B | HOH2033 |
| B | HOH2036 |
| B | HOH2059 |
| B | HOH2081 |
| B | HOH2107 |
| B | HOH2120 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 242 |
| 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 |
