3R1K
Crystal structure of acetyltransferase Eis from Mycobacterium tuberculosis H37Rv in complex with CoA and an acetamide moiety
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005829 | cellular_component | cytosol |
| A | 0008080 | molecular_function | N-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 | 0030649 | biological_process | aminoglycoside antibiotic catabolic process |
| A | 0033661 | biological_process | effector-mediated defense to host-produced reactive oxygen species |
| A | 0034069 | molecular_function | aminoglycoside N-acetyltransferase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043655 | cellular_component | host extracellular space |
| A | 0044161 | cellular_component | host cell cytoplasmic vesicle |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0051701 | biological_process | biological process involved in interaction with host |
| A | 0052032 | biological_process | symbiont-mediated perturbation of host inflammatory response |
| A | 0052040 | biological_process | symbiont-mediated perturbation of host programmed cell death |
| A | 0052041 | biological_process | symbiont-mediated suppression of host programmed cell death |
| A | 0052167 | biological_process | symbiont-mediated perturbation of host innate immune response |
| A | 0061733 | molecular_function | protein-lysine-acetyltransferase activity |
| A | 0097691 | cellular_component | bacterial extracellular vesicle |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE COA A 500 |
| Chain | Residue |
| A | VAL85 |
| A | ARG98 |
| A | SER121 |
| A | GLU122 |
| A | GLY124 |
| A | ILE125 |
| A | TYR126 |
| A | ARG128 |
| A | ASP260 |
| A | SER261 |
| A | ACM403 |
| A | ALA86 |
| A | HOH421 |
| A | HOH469 |
| A | HOH590 |
| A | HOH611 |
| A | HOH617 |
| A | VAL87 |
| A | ARG92 |
| A | ARG93 |
| A | ARG94 |
| A | GLY95 |
| A | LEU96 |
| A | LEU97 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACM A 403 |
| Chain | Residue |
| A | SER83 |
| A | PHE84 |
| A | VAL85 |
| A | HIS119 |
| A | TYR126 |
| A | COA500 |
| A | HOH669 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"21628583","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor; via carboxylate","evidences":[{"source":"PubMed","id":"21628583","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22547814","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21628583","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3RYO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22547814","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21628583","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24106131","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27010218","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3RYO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
