3U31
Plasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl lysine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000781 | cellular_component | chromosome, telomeric region |
| A | 0003677 | molecular_function | DNA binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005677 | cellular_component | chromatin silencing complex |
| A | 0005694 | cellular_component | chromosome |
| A | 0005730 | cellular_component | nucleolus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0006338 | biological_process | chromatin remodeling |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0016233 | biological_process | telomere capping |
| A | 0016740 | molecular_function | transferase activity |
| A | 0017136 | molecular_function | NAD-dependent histone 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAD A 274 |
| Chain | Residue |
| A | GLY36 |
| A | GLY207 |
| A | THR208 |
| A | SER209 |
| A | THR211 |
| A | VAL212 |
| A | ASN233 |
| A | ILE234 |
| A | LYS251 |
| A | PHE252 |
| A | HOH278 |
| A | SER37 |
| A | HOH281 |
| A | HOH318 |
| A | HOH337 |
| B | MYK9 |
| A | GLY38 |
| A | ALA41 |
| A | GLU42 |
| A | SER47 |
| A | ARG49 |
| A | GLN114 |
| A | PHE181 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 275 |
| Chain | Residue |
| A | SER37 |
| A | ARG49 |
| A | GLN114 |
| A | ASN115 |
| A | VAL116 |
| A | ASP117 |
| A | HOH337 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 276 |
| Chain | Residue |
| A | CYS140 |
| A | CYS143 |
| A | CYS168 |
| A | CYS170 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 |
| Chain | Residue | Details |
| B | LYS4 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594 |
| Chain | Residue | Details |
| A | PHE252 | |
| A | ASN233 | |
| B | GLN5 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790 |
| Chain | Residue | Details |
| A | GLY207 | |
| B | THR6 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433 |
| Chain | Residue | Details |
| B | ARG8 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 |
| Chain | Residue | Details |
| A | CYS143 | |
| A | CYS168 | |
| A | CYS170 | |
| B | MYK9 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16457588 |
| Chain | Residue | Details |
| B | SER10 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by PKC and CHEK1 => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:22901803 |
| Chain | Residue | Details |
| B | THR11 |
