6HD5
Cryo-EM structure of the ribosome-NatA complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| t | 0004596 | molecular_function | protein-N-terminal amino-acid acetyltransferase activity |
| t | 0005515 | molecular_function | protein binding |
| t | 0005737 | cellular_component | cytoplasm |
| t | 0005739 | cellular_component | mitochondrion |
| t | 0010698 | molecular_function | acetyltransferase activator activity |
| t | 0031415 | cellular_component | NatA complex |
| t | 0043022 | molecular_function | ribosome binding |
| u | 0004596 | molecular_function | protein-N-terminal amino-acid acetyltransferase activity |
| u | 0005515 | molecular_function | protein binding |
| u | 0005737 | cellular_component | cytoplasm |
| u | 0006474 | biological_process | N-terminal protein amino acid acetylation |
| u | 0008999 | molecular_function | protein-N-terminal-alanine acetyltransferase activity |
| u | 0016740 | molecular_function | transferase activity |
| u | 0016746 | molecular_function | acyltransferase activity |
| u | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| u | 0031415 | cellular_component | NatA complex |
| u | 0042802 | molecular_function | identical protein binding |
| u | 1990189 | molecular_function | protein N-terminal-serine acetyltransferase activity |
| u | 1990190 | molecular_function | protein-N-terminal-glutamate acetyltransferase activity |
| v | 0004596 | molecular_function | protein-N-terminal amino-acid acetyltransferase activity |
| v | 0005737 | cellular_component | cytoplasm |
| v | 0007064 | biological_process | mitotic sister chromatid cohesion |
| v | 0016740 | molecular_function | transferase activity |
| v | 0016746 | molecular_function | acyltransferase activity |
| v | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| v | 0031415 | cellular_component | NatA complex |
| v | 0120518 | molecular_function | protein N-terminal-methionine acetyltransferase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 33 |
| Details | Repeat: {"description":"TPR 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 33 |
| Details | Repeat: {"description":"TPR 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 33 |
| Details | Repeat: {"description":"TPR 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 36 |
| Details | Repeat: {"description":"TPR 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 33 |
| Details | Repeat: {"description":"TPR 5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 33 |
| Details | Repeat: {"description":"TPR 6"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 33 |
| Details | Repeat: {"description":"TPR 7"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 33 |
| Details | Repeat: {"description":"TPR 8"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 42 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 44 |
| Details | Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 160 |
| Details | Domain: {"description":"N-acetyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00532","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
