6AG4
Crystal structure of Ard1 N-terminal acetyltransferase H88A/E127A mutant from Sulfolobus solfataricus
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 | 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 24 |
Details | binding site for residue ACO A 201 |
Chain | Residue |
A | LEU33 |
A | GLY102 |
A | ILE103 |
A | ALA104 |
A | THR105 |
A | ALA127 |
A | ASN132 |
A | PRO134 |
A | LEU138 |
A | TYR139 |
A | LYS141 |
A | PHE74 |
A | HOH308 |
A | HOH317 |
A | HOH323 |
A | HOH334 |
A | HOH348 |
A | SER91 |
A | ILE92 |
A | ALA93 |
A | VAL94 |
A | ARG99 |
A | ARG100 |
A | LYS101 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue SO4 A 202 |
Chain | Residue |
A | SER61 |
A | VAL63 |
A | TRP72 |
A | LEU83 |
A | LEU95 |
A | TYR98 |
A | TYR133 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue CA A 203 |
Chain | Residue |
A | ARG129 |
A | ASN132 |
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 | ALA88 | |
A | ALA127 |
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 |