3JWP
Crystal structure of Plasmodium falciparum SIR2A (PF13_0152) in complex with AMP
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 | 12 |
Details | BINDING SITE FOR RESIDUE AMP A 266 |
Chain | Residue |
A | SER29 |
A | SER227 |
A | LYS243 |
A | PHE244 |
A | GLY30 |
A | GLU34 |
A | ARG41 |
A | GLY199 |
A | THR200 |
A | SER202 |
A | ASN225 |
A | ILE226 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 2001 |
Chain | Residue |
A | CYS132 |
A | CYS135 |
A | CYS160 |
A | CYS162 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PGE A 267 |
Chain | Residue |
A | PHE40 |
A | ILE171 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00236 |
Chain | Residue | Details |
A | HIS124 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03160, ECO:0000269|PubMed:21992006 |
Chain | Residue | Details |
A | GLY28 | |
A | ASN225 | |
A | PHE244 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03160 |
Chain | Residue | Details |
A | GLN106 | |
A | GLY199 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | HIS124 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03160, ECO:0000269|PubMed:21992006, ECO:0000269|Ref.14 |
Chain | Residue | Details |
A | CYS132 | |
A | CYS135 | |
A | CYS160 | |
A | CYS162 |