6WF5
Crystal structure of human Naa50 in complex with a truncated cofactor derived inhibitor (compound 2)
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 |
| B | 0004596 | molecular_function | protein-N-terminal amino-acid acetyltransferase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005730 | cellular_component | nucleolus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006338 | biological_process | chromatin remodeling |
| B | 0006474 | biological_process | N-terminal protein amino acid acetylation |
| B | 0007064 | biological_process | mitotic sister chromatid cohesion |
| B | 0010485 | molecular_function | histone H4 acetyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| B | 0031415 | cellular_component | NatA complex |
| B | 0034087 | biological_process | establishment of mitotic sister chromatid cohesion |
| B | 0043687 | biological_process | post-translational protein modification |
| B | 0061733 | molecular_function | protein-lysine-acetyltransferase activity |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0071962 | biological_process | mitotic sister chromatid cohesion, centromeric |
| B | 0120518 | molecular_function | protein N-terminal-methionine acetyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for Di-peptide ACE C 1 and MET C 2 |
| Chain | Residue |
| A | PHE27 |
| A | TYR139 |
| A | HOH207 |
| C | LEU3 |
| C | GLY4 |
| C | U44101 |
| A | PRO28 |
| A | TYR31 |
| A | MET75 |
| A | THR76 |
| A | LEU77 |
| A | LEU111 |
| A | HIS112 |
| A | GLN114 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for Di-peptide PRO C 5 and NH2 C 6 |
| Chain | Residue |
| A | VAL29 |
| A | TYR138 |
| A | LYS140 |
| A | ASP163 |
| C | GLY4 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | binding site for residues U44 C 101 and ACE C 1 |
| Chain | Residue |
| A | PHE27 |
| A | MET75 |
| A | THR76 |
| A | LEU77 |
| A | GLY78 |
| A | CYS79 |
| A | ARG84 |
| A | LEU111 |
| A | HIS112 |
| A | ASN117 |
| A | PHE123 |
| A | TYR124 |
| A | HOH231 |
| C | MET2 |
| C | HOH201 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for Di-peptide ACE G 1 and MET G 2 |
| Chain | Residue |
| B | PHE27 |
| B | PRO28 |
| B | TYR31 |
| B | MET75 |
| B | THR76 |
| B | LEU77 |
| B | LEU111 |
| B | HIS112 |
| B | TYR139 |
| D | LEU3 |
| D | GLY4 |
| D | U44101 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for Di-peptide PRO G 5 and NH2 G 6 |
| Chain | Residue |
| B | TYR138 |
| D | GLY4 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | binding site for residues U44 G 101 and ACE G 1 |
| Chain | Residue |
| B | PHE27 |
| B | MET75 |
| B | THR76 |
| B | LEU77 |
| B | GLY78 |
| B | CYS79 |
| B | ARG84 |
| B | LEU111 |
| B | HIS112 |
| B | ASN117 |
| B | SER119 |
| B | PHE123 |
| B | TYR124 |
| D | MET2 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 298 |
| Details | Domain: {"description":"N-acetyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00532","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"21900231","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| 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_FI4 |
| Number of Residues | 44 |
| 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_FI5 |
| Number of Residues | 2 |
| 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_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| 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_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"19744929","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
