6WFN
Crystal structure of human Naa50 in complex with AcCoA and an inhibitor (compound 4a) identified using DNA encoded library technology
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004596 | molecular_function | peptide alpha-N-acetyltransferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005730 | cellular_component | nucleolus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006338 | biological_process | chromatin remodeling |
| A | 0006474 | biological_process | N-terminal protein amino acid acetylation |
| A | 0007064 | biological_process | mitotic sister chromatid cohesion |
| A | 0010485 | molecular_function | histone H4 acetyltransferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| A | 0031415 | cellular_component | NatA complex |
| A | 0034087 | biological_process | establishment of mitotic sister chromatid cohesion |
| A | 0061733 | molecular_function | peptide-lysine-N-acetyltransferase activity |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0071962 | biological_process | mitotic sister chromatid cohesion, centromeric |
| A | 0120518 | molecular_function | peptide-methionine-alpha-N-acetyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 34 |
| Details | binding site for residue ACO A 201 |
| Chain | Residue |
| A | ILE26 |
| A | CYS79 |
| A | ARG84 |
| A | ARG85 |
| A | LEU86 |
| A | GLY87 |
| A | ILE88 |
| A | GLY89 |
| A | THR90 |
| A | ASN117 |
| A | SER119 |
| A | PHE27 |
| A | ALA120 |
| A | PHE123 |
| A | TYR124 |
| A | LYS126 |
| A | U2J202 |
| A | HOH301 |
| A | HOH304 |
| A | HOH307 |
| A | HOH322 |
| A | HOH333 |
| A | ARG62 |
| A | HOH353 |
| A | HOH401 |
| A | HOH402 |
| A | HOH411 |
| A | HOH433 |
| A | ASP64 |
| A | HIS65 |
| A | ILE74 |
| A | THR76 |
| A | LEU77 |
| A | GLY78 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | binding site for residue U2J A 202 |
| Chain | Residue |
| A | PHE27 |
| A | PRO28 |
| A | VAL29 |
| A | TYR31 |
| A | TYR73 |
| A | MET75 |
| A | ARG85 |
| A | HIS112 |
| A | VAL113 |
| A | GLN114 |
| A | TYR138 |
| A | TYR139 |
| A | LYS140 |
| A | ARG141 |
| A | ACO201 |
| A | HOH310 |
| A | HOH321 |
| A | HOH350 |
| A | HOH360 |
| A | HOH387 |
| A | HOH427 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:21900231 |
| Chain | Residue | Details |
| A | TYR73 | |
| A | HIS112 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21900231, ECO:0000269|PubMed:27484799, ECO:0007744|PDB:3TFY, ECO:0007744|PDB:4X5K |
| Chain | Residue | Details |
| A | TYR31 | |
| A | MET75 | |
| A | TYR138 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21900231, ECO:0000269|PubMed:27484799, ECO:0000269|Ref.19, ECO:0007744|PDB:2PSW, ECO:0007744|PDB:3TFY, ECO:0007744|PDB:4X5K |
| Chain | Residue | Details |
| A | LEU77 | |
| A | ASN117 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | THR12 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:19744929, ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS34 | |
| A | LYS37 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455 |
| Chain | Residue | Details |
| A | TYR110 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:19744929 |
| Chain | Residue | Details |
| A | LYS140 |
