6WFG
Crystal structure of human Naa50 in complex with an inhibitor (compound 3) 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 | ||
C | 0004596 | molecular_function | peptide alpha-N-acetyltransferase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005634 | cellular_component | nucleus |
C | 0005730 | cellular_component | nucleolus |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006338 | biological_process | chromatin remodeling |
C | 0006474 | biological_process | N-terminal protein amino acid acetylation |
C | 0007064 | biological_process | mitotic sister chromatid cohesion |
C | 0010485 | molecular_function | histone H4 acetyltransferase activity |
C | 0016746 | molecular_function | acyltransferase activity |
C | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
C | 0031415 | cellular_component | NatA complex |
C | 0034087 | biological_process | establishment of mitotic sister chromatid cohesion |
C | 0061733 | molecular_function | peptide-lysine-N-acetyltransferase activity |
C | 0070062 | cellular_component | extracellular exosome |
C | 0071962 | biological_process | mitotic sister chromatid cohesion, centromeric |
C | 0120518 | ||
E | 0004596 | molecular_function | peptide alpha-N-acetyltransferase activity |
E | 0005515 | molecular_function | protein binding |
E | 0005634 | cellular_component | nucleus |
E | 0005730 | cellular_component | nucleolus |
E | 0005737 | cellular_component | cytoplasm |
E | 0005829 | cellular_component | cytosol |
E | 0006338 | biological_process | chromatin remodeling |
E | 0006474 | biological_process | N-terminal protein amino acid acetylation |
E | 0007064 | biological_process | mitotic sister chromatid cohesion |
E | 0010485 | molecular_function | histone H4 acetyltransferase activity |
E | 0016746 | molecular_function | acyltransferase activity |
E | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
E | 0031415 | cellular_component | NatA complex |
E | 0034087 | biological_process | establishment of mitotic sister chromatid cohesion |
E | 0061733 | molecular_function | peptide-lysine-N-acetyltransferase activity |
E | 0070062 | cellular_component | extracellular exosome |
E | 0071962 | biological_process | mitotic sister chromatid cohesion, centromeric |
E | 0120518 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 20 |
Details | binding site for residue COA A 201 |
Chain | Residue |
A | PHE27 |
A | GLY89 |
A | THR90 |
A | ASN117 |
A | SER119 |
A | ASP122 |
A | PHE123 |
A | LYS126 |
A | HOH301 |
A | HOH302 |
A | HOH304 |
A | LEU77 |
A | HOH313 |
A | GLY78 |
A | CYS79 |
A | ARG84 |
A | ARG85 |
A | LEU86 |
A | GLY87 |
A | ILE88 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue U3V A 202 |
Chain | Residue |
A | VAL29 |
A | TYR31 |
A | ARG62 |
A | ASP64 |
A | TYR73 |
A | MET75 |
A | TYR110 |
A | HIS112 |
A | GLN114 |
A | TYR138 |
A | TYR139 |
site_id | AC3 |
Number of Residues | 20 |
Details | binding site for residue COA C 201 |
Chain | Residue |
C | PHE27 |
C | LEU77 |
C | GLY78 |
C | CYS79 |
C | ARG84 |
C | ARG85 |
C | LEU86 |
C | GLY87 |
C | ILE88 |
C | GLY89 |
C | THR90 |
C | ASN117 |
C | SER119 |
C | ASP122 |
C | PHE123 |
C | LYS126 |
C | HOH301 |
C | HOH303 |
C | HOH306 |
C | HOH308 |
site_id | AC4 |
Number of Residues | 12 |
Details | binding site for residue U3V C 202 |
Chain | Residue |
C | TYR31 |
C | ARG62 |
C | ASP64 |
C | TYR73 |
C | MET75 |
C | TYR110 |
C | HIS112 |
C | VAL113 |
C | GLN114 |
C | TYR138 |
C | TYR139 |
C | HOH310 |
site_id | AC5 |
Number of Residues | 19 |
Details | binding site for residue COA E 201 |
Chain | Residue |
E | PHE27 |
E | LEU77 |
E | GLY78 |
E | CYS79 |
E | ARG84 |
E | ARG85 |
E | LEU86 |
E | GLY87 |
E | GLY89 |
E | THR90 |
E | ASN117 |
E | SER119 |
E | ASP122 |
E | PHE123 |
E | TYR124 |
E | LYS126 |
E | HOH301 |
E | HOH302 |
E | HOH305 |
site_id | AC6 |
Number of Residues | 13 |
Details | binding site for residue U3V E 202 |
Chain | Residue |
E | VAL29 |
E | TYR31 |
E | ARG62 |
E | ASP64 |
E | TYR73 |
E | MET75 |
E | TYR110 |
E | HIS112 |
E | VAL113 |
E | GLN114 |
E | TYR138 |
E | TYR139 |
E | HOH311 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:21900231 |
Chain | Residue | Details |
A | TYR73 | |
A | HIS112 | |
C | TYR73 | |
C | HIS112 | |
E | TYR73 | |
E | HIS112 |
site_id | SWS_FT_FI2 |
Number of Residues | 9 |
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 | |
C | TYR31 | |
C | MET75 | |
C | TYR138 | |
E | TYR31 | |
E | MET75 | |
E | TYR138 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
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 | |
C | LEU77 | |
C | ASN117 | |
E | LEU77 | |
E | ASN117 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | THR12 | |
C | THR12 | |
E | THR12 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | MOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:19744929, ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS34 | |
A | LYS37 | |
C | LYS34 | |
C | LYS37 | |
E | LYS34 | |
E | LYS37 |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455 |
Chain | Residue | Details |
A | TYR110 | |
C | TYR110 | |
E | TYR110 |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | MOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:19744929 |
Chain | Residue | Details |
A | LYS140 | |
C | LYS140 | |
E | LYS140 |