6O07
Structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex
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 | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0010698 | molecular_function | acetyltransferase activator activity |
A | 0031415 | cellular_component | NatA complex |
A | 0043022 | molecular_function | ribosome binding |
B | 0004596 | molecular_function | peptide alpha-N-acetyltransferase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006474 | biological_process | N-terminal protein amino acid acetylation |
B | 0008999 | molecular_function | peptide-alanine-alpha-N-acetyltransferase 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 | 0042802 | molecular_function | identical protein binding |
B | 1990189 | molecular_function | peptide-serine-alpha-N-acetyltransferase activity |
B | 1990190 | molecular_function | peptide-glutamate-alpha-N-acetyltransferase activity |
C | 0004596 | molecular_function | peptide alpha-N-acetyltransferase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0007064 | biological_process | mitotic sister chromatid cohesion |
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 | 0120518 | molecular_function | peptide-methionine-alpha-N-acetyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | binding site for residue CL C 201 |
Chain | Residue |
C | GLN166 |
C | ASP167 |
site_id | AC2 |
Number of Residues | 1 |
Details | binding site for residue GOL C 202 |
Chain | Residue |
C | PHE60 |
site_id | AC3 |
Number of Residues | 17 |
Details | binding site for residue ACO C 203 |
Chain | Residue |
C | HIS104 |
C | SER106 |
C | ILE107 |
C | GLY108 |
C | SER109 |
C | TYR130 |
C | THR138 |
C | TRP141 |
C | PHE142 |
C | HOH304 |
C | HOH307 |
C | GLU94 |
C | PHE95 |
C | LEU96 |
C | GLY97 |
C | VAL98 |
C | ARG103 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue CL A 901 |
Chain | Residue |
A | TYR511 |
A | LYS515 |
site_id | AC5 |
Number of Residues | 1 |
Details | binding site for residue CL A 902 |
Chain | Residue |
A | GLN617 |
site_id | AC6 |
Number of Residues | 1 |
Details | binding site for residue CL A 903 |
Chain | Residue |
A | GLU693 |
site_id | AC7 |
Number of Residues | 1 |
Details | binding site for residue CL A 906 |
Chain | Residue |
A | GLU443 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue CL A 908 |
Chain | Residue |
A | LYS609 |
A | SER612 |
site_id | AC9 |
Number of Residues | 1 |
Details | binding site for residue CL A 909 |
Chain | Residue |
A | TYR722 |
site_id | AD1 |
Number of Residues | 1 |
Details | binding site for residue CL A 910 |
Chain | Residue |
A | ARG708 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue GOL A 912 |
Chain | Residue |
A | TYR508 |
A | ARG509 |
A | LYS613 |
A | GLU848 |
A | TYR853 |
A | GOL916 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue GOL A 913 |
Chain | Residue |
A | ASN180 |
A | ASP435 |
A | GLY439 |
A | PHE462 |
A | HOH1069 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue GOL A 914 |
Chain | Residue |
A | LYS470 |
A | GLU473 |
A | HOH1013 |
site_id | AD5 |
Number of Residues | 2 |
Details | binding site for residue GOL A 915 |
Chain | Residue |
A | ILE810 |
A | LEU841 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue GOL A 916 |
Chain | Residue |
A | ARG464 |
A | ARG509 |
A | HIS844 |
A | GLU848 |
A | GOL912 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue MLI A 917 |
Chain | Residue |
A | LEU431 |
A | PRO843 |
A | GLN846 |
A | ASN847 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue MLI A 918 |
Chain | Residue |
A | LYS149 |
A | GLU153 |
A | THR436 |
site_id | AD9 |
Number of Residues | 4 |
Details | binding site for residue MLI A 919 |
Chain | Residue |
A | HIS201 |
A | ASP232 |
A | ILE233 |
A | CYS236 |
site_id | AE1 |
Number of Residues | 12 |
Details | binding site for residue IHP A 920 |
Chain | Residue |
A | SER346 |
A | LYS349 |
A | ARG426 |
A | LYS429 |
A | HIS430 |
A | LYS457 |
A | LYS460 |
A | TYR461 |
A | ARG464 |
B | LYS80 |
B | TYR85 |
B | LYS91 |
site_id | AE2 |
Number of Residues | 1 |
Details | binding site for residue CL B 302 |
Chain | Residue |
B | ASP223 |
site_id | AE3 |
Number of Residues | 3 |
Details | binding site for residue CL B 305 |
Chain | Residue |
B | ASN158 |
B | ALA161 |
B | EPE310 |
site_id | AE4 |
Number of Residues | 5 |
Details | binding site for residue CL B 306 |
Chain | Residue |
B | HIS163 |
B | LEU164 |
B | THR168 |
B | HOH429 |
B | HOH441 |
site_id | AE5 |
Number of Residues | 4 |
Details | binding site for residue GOL B 307 |
Chain | Residue |
B | HIS114 |
B | THR116 |
B | HIS153 |
B | TYR180 |
site_id | AE6 |
Number of Residues | 4 |
Details | binding site for residue GOL B 308 |
Chain | Residue |
A | PHE453 |
B | ALA19 |
B | HIS22 |
B | MET121 |
site_id | AE7 |
Number of Residues | 5 |
Details | binding site for residue MLI B 309 |
Chain | Residue |
B | SER117 |
B | LEU118 |
B | HIS153 |
B | TYR165 |
B | HOH411 |
site_id | AE8 |
Number of Residues | 11 |
Details | binding site for residue EPE B 310 |
Chain | Residue |
B | GLY128 |
B | ILE129 |
B | ALA130 |
B | GLU131 |
B | ALA160 |
B | LEU164 |
B | CL305 |
B | VAL120 |
B | ARG125 |
B | ARG126 |
B | MET127 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylserine => ECO:0000255 |
Chain | Residue | Details |
A | SER2 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956 |
Chain | Residue | Details |
A | SER674 |