4R3K
Crystal structure of Ard1 N-terminal acetyltransferase from Sulfolobus solfataricus bound to CoA
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 | 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 | 0046872 | molecular_function | metal ion binding |
| A | 1990189 | molecular_function | peptide-serine-alpha-N-acetyltransferase activity |
| A | 1990190 | molecular_function | peptide-glutamate-alpha-N-acetyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE COA A 400 |
| Chain | Residue |
| A | LEU33 |
| A | ILE103 |
| A | ALA104 |
| A | THR105 |
| A | GLU127 |
| A | ASN132 |
| A | TYR133 |
| A | PRO134 |
| A | ALA137 |
| A | LEU138 |
| A | TYR139 |
| A | LYS47 |
| A | LYS141 |
| A | CA403 |
| A | HOH501 |
| A | HOH506 |
| A | HOH524 |
| A | HOH527 |
| A | HOH531 |
| A | ILE92 |
| A | ALA93 |
| A | VAL94 |
| A | ARG99 |
| A | ARG100 |
| A | LYS101 |
| A | GLY102 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 401 |
| Chain | Residue |
| A | ARG18 |
| A | MET19 |
| A | LYS141 |
| A | HOH514 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 402 |
| Chain | Residue |
| A | GLU35 |
| A | ARG129 |
| A | TYR154 |
| A | ALA155 |
| A | ASP156 |
| A | HOH513 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA A 403 |
| Chain | Residue |
| A | ARG129 |
| A | ASN132 |
| A | COA400 |
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 | TYR37 | |
| A | TYR154 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23959863, ECO:0007744|PDB:4LX9 |
| Chain | Residue | Details |
| A | HIS88 | |
| A | GLU127 |
| 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 | ILE92 | |
| A | ARG100 |
| 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 | ASN132 | |
| A | TYR139 |
| 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 | GLU35 |
| 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 | SER75 | |
| A | SER82 |
