2ZPA
Crystal Structure of tRNA(Met) Cytidine Acetyltransferase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0002101 | biological_process | tRNA wobble cytosine modification |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008033 | biological_process | tRNA processing |
| 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 | 0051391 | biological_process | tRNA acetylation |
| A | 0051392 | molecular_function | tRNA N-acetyltransferase activity |
| A | 0106226 | molecular_function | peptide 2-hydroxyisobutyryltransferase activity |
| B | 0000049 | molecular_function | tRNA binding |
| B | 0002101 | biological_process | tRNA wobble cytosine modification |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008033 | biological_process | tRNA processing |
| B | 0008080 | molecular_function | N-acetyltransferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| B | 0051391 | biological_process | tRNA acetylation |
| B | 0051392 | molecular_function | tRNA N-acetyltransferase activity |
| B | 0106226 | molecular_function | peptide 2-hydroxyisobutyryltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 801 |
| Chain | Residue |
| B | ARG201 |
| B | GLY202 |
| B | ARG203 |
| B | GLY204 |
| B | LYS205 |
| B | SER206 |
| B | HOH979 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ACO A 700 |
| Chain | Residue |
| A | ILE461 |
| A | GLN468 |
| A | ARG469 |
| A | GLU470 |
| A | GLY471 |
| A | THR472 |
| A | GLY473 |
| A | ARG474 |
| A | SER493 |
| A | GLU499 |
| A | ARG502 |
| A | PHE503 |
| A | ARG506 |
| A | HOH875 |
| A | HOH887 |
| A | SER459 |
| A | ARG460 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ACO B 701 |
| Chain | Residue |
| B | LYS301 |
| B | SER459 |
| B | ILE461 |
| B | ARG469 |
| B | GLU470 |
| B | GLY471 |
| B | THR472 |
| B | GLY473 |
| B | ARG474 |
| B | SER493 |
| B | PHE494 |
| B | LEU500 |
| B | PHE503 |
| B | ARG506 |
| B | HOH906 |
| B | HOH930 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ADP A 800 |
| Chain | Residue |
| A | ALA172 |
| A | GLY174 |
| A | ALA175 |
| A | PRO176 |
| A | GLN180 |
| A | ALA200 |
| A | GLY202 |
| A | ARG203 |
| A | GLY204 |
| A | LYS205 |
| A | SER206 |
| A | ALA207 |
| A | GLN211 |
| A | PHE236 |
| A | ILE318 |
| A | ARG319 |
| A | HOH856 |
| A | HOH908 |
| A | HOH968 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01886, ECO:0000269|PubMed:19322199 |
| Chain | Residue | Details |
| A | GLN180 | |
| B | ARG319 | |
| B | ILE461 | |
| B | GLN468 | |
| B | GLU499 | |
| B | ARG506 | |
| A | GLY202 | |
| A | ARG319 | |
| A | ILE461 | |
| A | GLN468 | |
| A | GLU499 | |
| A | ARG506 | |
| B | GLN180 | |
| B | GLY202 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | SITE: Important for lysine 2-hydroxyisobutyryltransferase activity => ECO:0000305|PubMed:34903851 |
| Chain | Residue | Details |
| A | ARG502 | |
| B | ARG502 |
