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 | 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 | 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 | 1 |
Details | MOD_RES: N-acetylserine; by ard1 acetylase => ECO:0000269|PubMed:11935028, ECO:0000269|PubMed:17511810, ECO:0000269|PubMed:29679495 |
Chain | Residue | Details |
B | SER1 | |
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 |