2X7B
Crystal structure of the N-terminal acetylase Ard1 from Sulfolobus solfataricus P2
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 | 25 |
Details | BINDING SITE FOR RESIDUE COA A 201 |
Chain | Residue |
A | LEU33 |
A | ALA104 |
A | THR105 |
A | GLU127 |
A | ASN132 |
A | PRO134 |
A | ALA137 |
A | LEU138 |
A | TYR139 |
A | LYS141 |
A | ARG165 |
A | ILE92 |
A | HOH2020 |
A | HOH2029 |
A | HOH2039 |
A | HOH2048 |
A | HOH2066 |
A | HOH2067 |
A | ALA93 |
A | VAL94 |
A | ARG99 |
A | ARG100 |
A | LYS101 |
A | GLY102 |
A | ILE103 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL A 202 |
Chain | Residue |
A | ARG129 |
A | TYR154 |
A | ALA155 |
A | ASP156 |
A | GLY157 |
A | GLU158 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
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_FI2 |
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_FI3 |
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_FI4 |
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_FI5 |
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_FI6 |
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 |