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 | 0008270 | molecular_function | zinc ion binding |
A | 0016740 | molecular_function | transferase activity |
A | 0017136 | molecular_function | NAD-dependent histone deacetylase activity |
A | 0033558 | molecular_function | protein lysine deacetylase activity |
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 | NAD-dependent histone deacetylase activity |
B | 0033558 | molecular_function | protein lysine deacetylase activity |
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 | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00236 |
Chain | Residue | Details |
A | HIS116 | |
B | HIS116 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676 |
Chain | Residue | Details |
A | GLY20 | |
B | ALA229 | |
A | GLN98 | |
A | GLY185 | |
A | ASN211 | |
A | ALA229 | |
B | GLY20 | |
B | GLN98 | |
B | GLY185 | |
B | ASN211 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01121 |
Chain | Residue | Details |
A | TYR64 | |
A | ARG67 | |
B | TYR64 | |
B | ARG67 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676, ECO:0000269|PubMed:12091395 |
Chain | Residue | Details |
A | CYS124 | |
A | CYS127 | |
A | CYS145 | |
A | CYS148 | |
B | CYS124 | |
B | CYS127 | |
B | CYS145 | |
B | CYS148 |