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 | protein-N-terminal amino-acid 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 | 0016740 | molecular_function | transferase 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 | 0043687 | biological_process | post-translational protein modification |
| A | 0061733 | molecular_function | protein-lysine-acetyltransferase activity |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0071962 | biological_process | mitotic sister chromatid cohesion, centromeric |
| A | 0120518 | molecular_function | protein N-terminal-methionine 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 | Active site: {"evidences":[{"source":"PubMed","id":"21900231","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21900231","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27484799","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3TFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4X5K","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21900231","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27484799","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2007","submissionDatabase":"PDB data bank","title":"Structure of human MAK3 homolog.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2PSW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4X5K","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"19744929","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"19744929","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
