4LX9
Archaeal amino-terminal acetyltransferase (NAT) bound to acetyl coenzyme A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004596 | molecular_function | peptide alpha-N-acetyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006474 | biological_process | N-terminal protein amino acid acetylation |
| A | 0008080 | molecular_function | N-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 | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE ACO A 301 |
| Chain | Residue |
| A | THR81 |
| A | LYS150 |
| A | GLY151 |
| A | ILE152 |
| A | ALA153 |
| A | THR154 |
| A | GLU176 |
| A | ASN181 |
| A | TYR182 |
| A | PRO183 |
| A | LEU187 |
| A | LEU82 |
| A | TYR188 |
| A | LYS190 |
| A | ARG214 |
| A | HOH410 |
| A | HOH411 |
| A | HOH415 |
| A | HOH427 |
| A | HOH461 |
| A | HOH475 |
| A | HOH496 |
| A | VAL138 |
| A | HOH515 |
| A | HOH528 |
| A | HOH536 |
| A | HOH538 |
| A | SER140 |
| A | ILE141 |
| A | ALA142 |
| A | VAL143 |
| A | ARG148 |
| A | ARG149 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 302 |
| Chain | Residue |
| A | HIS137 |
| A | GLU176 |
| A | HOH405 |
| A | HOH412 |
| A | HOH520 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN A 303 |
| Chain | Residue |
| A | GLU145 |
| A | ASP167 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25728374, ECO:0007744|PDB:4R3L |
| Chain | Residue | Details |
| A | TYR86 | |
| A | TYR203 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23959863, ECO:0007744|PDB:4LX9 |
| Chain | Residue | Details |
| A | HIS137 | |
| A | GLU176 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20419351, ECO:0000269|PubMed:23959863, ECO:0000269|PubMed:25728374, ECO:0000269|PubMed:26593285, ECO:0007744|PDB:2X7B, ECO:0007744|PDB:4LX9, ECO:0007744|PDB:4R3K, ECO:0007744|PDB:4R3L, ECO:0007744|PDB:5C88 |
| Chain | Residue | Details |
| A | ILE141 | |
| A | ARG149 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20419351, ECO:0000269|PubMed:23959863, ECO:0000269|PubMed:25728374, ECO:0007744|PDB:2X7B, ECO:0007744|PDB:4LX9, ECO:0007744|PDB:4R3K, ECO:0007744|PDB:4R3L |
| Chain | Residue | Details |
| A | ASN181 | |
| A | TYR188 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | SITE: Plays an important role in substrate specificity => ECO:0000269|PubMed:25728374 |
| Chain | Residue | Details |
| A | GLU84 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Plays an important role in modulating multiple conformations of loop regions and contributes to protein thermostability => ECO:0000269|PubMed:26593285 |
| Chain | Residue | Details |
| A | SER124 | |
| A | SER131 |
