6VUR
Crystal structure of Eis from Mycobacterium tuberculosis in complex with inhibitor SGT366
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 | 5 |
| Details | binding site for residue ROG A 501 |
| Chain | Residue |
| A | ASP26 |
| A | TRP36 |
| A | SER83 |
| A | PHE84 |
| A | PHE402 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 502 |
| Chain | Residue |
| A | TRP13 |
| A | ARG37 |
| A | VAL40 |
| A | PRO41 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 503 |
| Chain | Residue |
| A | GLY73 |
| A | GLY309 |
| A | TYR310 |
| A | ASP393 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | ARG297 |
| A | MET299 |
| A | ARG353 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 505 |
| Chain | Residue |
| A | PHE24 |
| A | PHE84 |
| A | VAL85 |
| A | HIS119 |
| A | ALA120 |
| A | SER121 |
| A | TYR126 |
| A | HOH740 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue PEG A 506 |
| Chain | Residue |
| A | THR136 |
| A | PRO271 |
| A | GLN272 |
| A | ALA363 |
| A | VAL396 |
| A | HOH632 |
| A | HOH638 |
| A | HOH650 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue PEG A 507 |
| Chain | Residue |
| A | LEU241 |
| A | THR269 |
| A | HIS270 |
| A | PRO274 |
| A | GLN397 |
| A | SO4510 |
| A | HOH619 |
| A | HOH713 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 508 |
| Chain | Residue |
| A | ALA134 |
| A | SER358 |
| A | LEU361 |
| A | GLY362 |
| A | ALA363 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 509 |
| Chain | Residue |
| A | THR136 |
| A | HIS270 |
| A | THR398 |
| A | SO4510 |
| A | HOH632 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 A 510 |
| Chain | Residue |
| A | ARG242 |
| A | ILE268 |
| A | THR269 |
| A | HIS270 |
| A | GLN397 |
| A | THR398 |
| A | PEG507 |
| A | NA509 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 511 |
| Chain | Residue |
| A | ARG68 |
| A | LEU69 |
| A | THR70 |
| A | ARG183 |
| A | GLY189 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue CL A 512 |
| Chain | Residue |
| A | HIS150 |
| A | ALA153 |
| A | HIS277 |
| A | LEU278 |
| A | ALA372 |
| A | ARG374 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 513 |
| Chain | Residue |
| A | THR42 |
| A | TYR64 |
| A | TYR113 |
| A | PRO342 |
| A | THR343 |
| A | ASP344 |
| A | HOH625 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 514 |
| Chain | Residue |
| A | GLY95 |
| A | ARG98 |
| A | HOH726 |
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 |
