4R3L
Crystal structure of Ard1 N-terminal acetyltransferase from Sulfolobus solfataricus bound to substrate peptide fragment and CoA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004596 | molecular_function | protein-N-terminal amino-acid 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 | 0008999 | molecular_function | protein-N-terminal-alanine 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 | 0120518 | molecular_function | protein N-terminal-methionine acetyltransferase activity |
| A | 1990189 | molecular_function | protein N-terminal-serine acetyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE COA A 400 |
| Chain | Residue |
| A | THR32 |
| A | GLY102 |
| A | ILE103 |
| A | ALA104 |
| A | THR105 |
| A | ASN132 |
| A | TYR133 |
| A | PRO134 |
| A | ALA137 |
| A | LEU138 |
| A | TYR139 |
| A | LEU33 |
| A | LYS141 |
| A | HOH502 |
| A | HOH526 |
| A | HOH528 |
| A | HOH540 |
| A | HOH568 |
| A | HOH584 |
| B | SER1 |
| A | LYS47 |
| A | ILE92 |
| A | ALA93 |
| A | VAL94 |
| A | ARG99 |
| A | ARG100 |
| A | LYS101 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR CHAIN B OF N-TERMINAL 6-MER PEPTIDE FROM ALBA |
| Chain | Residue |
| A | GLU35 |
| A | TYR37 |
| A | HIS88 |
| A | VAL89 |
| A | VAL90 |
| A | GLU127 |
| A | VAL128 |
| A | TYR153 |
| A | TYR154 |
| A | COA400 |
| A | HOH520 |
| A | HOH585 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 155 |
| Details | Domain: {"description":"N-acetyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00532","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25728374","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4R3L","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23959863","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LX9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20419351","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23959863","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25728374","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26593285","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2X7B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4LX9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4R3K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4R3L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5C88","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20419351","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23959863","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25728374","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2X7B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4LX9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4R3K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4R3L","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Plays an important role in substrate specificity","evidences":[{"source":"PubMed","id":"25728374","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Site: {"description":"Plays an important role in modulating multiple conformations of loop regions and contributes to protein thermostability","evidences":[{"source":"PubMed","id":"26593285","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylserine; by ard1 acetylase","evidences":[{"source":"PubMed","id":"11935028","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17511810","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29679495","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
