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 | 0005829 | cellular_component | cytosol |
| 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 | 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 | 0061697 | molecular_function | protein-glutaryllysine deglutarylase activity |
| A | 0070403 | molecular_function | NAD+ binding |
| A | 0141218 | molecular_function | NAD-dependent protein lysine deacylase activity |
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 | 254 |
| 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 | 1 |
| 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 | 23 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03160","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21992006","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03160","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03160","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21992006","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of Plasmodium falciparum SIR2A (PF13_0152) in complex with AMP.","authoringGroup":["Structural genomics consortium (SGC)"],"authors":["Wernimont A.K.","Hutchinson A.","Lin Y.H.","MacKenzie F.","Senisterra G.","Allali-Hassanali A.","Vedadi M.","Ravichandran M.","Cossar D.","Kozieradzki I.","Zhao Y.","Schapira M.","Arrowsmith C.H.","Bountra C.","Weigelt J.","Edwards A.M.","Hui R.","Qiu W.","Brand V."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by PKC","evidences":[{"source":"PubMed","id":"20228790","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Symmetric dimethylarginine; by PRMT5; alternate","evidences":[{"source":"UniProtKB","id":"P68433","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"11242053","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16185088","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16267050","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16457588","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17194708","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
