4XNH
Crystal structure of yeast N-terminal acetyltransferase NatE (IP6) in complex with a bisubstrate
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 | 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 | 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | binding site for residue IHP A 901 |
| Chain | Residue |
| A | LYS349 |
| A | HOH1002 |
| A | HOH1031 |
| A | HOH1093 |
| A | HOH1128 |
| A | HOH1214 |
| A | HOH1221 |
| A | HOH1290 |
| A | HOH1333 |
| B | LYS80 |
| B | TYR85 |
| A | ILE422 |
| B | LYS91 |
| B | THR123 |
| B | TYR124 |
| A | ARG426 |
| A | LYS429 |
| A | HIS430 |
| A | LYS457 |
| A | LYS460 |
| A | TYR461 |
| A | ARG464 |
| site_id | AC2 |
| Number of Residues | 27 |
| Details | binding site for residue ACO C 201 |
| Chain | Residue |
| A | GLN320 |
| A | HOH1037 |
| A | HOH1091 |
| C | THR26 |
| C | TYR31 |
| C | ILE93 |
| C | GLU94 |
| C | PHE95 |
| C | LEU96 |
| C | GLY97 |
| C | VAL98 |
| C | ARG103 |
| C | HIS104 |
| C | LYS105 |
| C | SER106 |
| C | ILE107 |
| C | GLY108 |
| C | SER109 |
| C | TYR130 |
| C | TRP141 |
| C | HOH301 |
| C | HOH316 |
| C | HOH320 |
| C | HOH321 |
| C | HOH322 |
| C | HOH323 |
| C | HOH324 |
| site_id | AC3 |
| Number of Residues | 32 |
| Details | binding site for residue CMC F 301 |
| Chain | Residue |
| B | ASN23 |
| B | LEU24 |
| B | SER117 |
| B | LEU118 |
| B | SER119 |
| B | VAL120 |
| B | ARG125 |
| B | ARG126 |
| B | MET127 |
| B | GLY128 |
| B | ILE129 |
| B | ALA130 |
| B | GLU131 |
| B | HIS153 |
| B | VAL154 |
| B | ASN158 |
| B | ALA160 |
| B | HIS163 |
| B | TYR165 |
| B | THR168 |
| B | ARG207 |
| B | HOH305 |
| B | HOH326 |
| C | GLU68 |
| F | SER1 |
| F | HOH401 |
| F | HOH404 |
| F | HOH405 |
| F | HOH406 |
| F | HOH407 |
| F | HOH408 |
| F | HOH411 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylserine; in Corticotropin => ECO:0000250|UniProtKB:P01191 |
| Chain | Residue | Details |
| F | SER1 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956 |
| Chain | Residue | Details |
| A | SER674 |
