6VV1
Crystal structure of Eis from Mycobacterium tuberculosis in complex with inhibitor SGT384
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 | 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 | 0034054 | biological_process | symbiont-mediated suppression of host defense-related programmed cell death |
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 | 0052167 | biological_process | symbiont-mediated perturbation of host innate immune response |
A | 0061733 | molecular_function | peptide-lysine-N-acetyltransferase activity |
A | 0097691 | cellular_component | bacterial extracellular vesicle |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue RMJ A 501 |
Chain | Residue |
A | PHE24 |
A | ASP26 |
A | TRP36 |
A | MET65 |
A | SER83 |
A | PHE84 |
A | GLU401 |
A | PHE402 |
A | HOH652 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue PEG A 502 |
Chain | Residue |
A | ALA177 |
A | ARG192 |
A | GLN194 |
A | GOL504 |
A | HOH671 |
site_id | AC3 |
Number of Residues | 10 |
Details | binding site for residue PEG A 503 |
Chain | Residue |
A | LEU241 |
A | ARG242 |
A | ILE267 |
A | ILE268 |
A | THR269 |
A | HIS270 |
A | ASP273 |
A | DMS511 |
A | HOH648 |
A | HOH715 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue GOL A 504 |
Chain | Residue |
A | GLN194 |
A | PEG502 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue GOL A 505 |
Chain | Residue |
A | HIS105 |
A | ARG297 |
A | MET299 |
A | HOH614 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 506 |
Chain | Residue |
A | GLY73 |
A | ALA391 |
A | ASP393 |
A | HOH633 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 507 |
Chain | Residue |
A | TRP13 |
A | VAL40 |
A | PRO41 |
A | ALA45 |
A | HOH612 |
A | HOH626 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue GOL A 508 |
Chain | Residue |
A | ARG37 |
A | THR38 |
A | VAL40 |
A | ASP344 |
A | HOH716 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue DMS A 509 |
Chain | Residue |
A | GLU139 |
A | TRP289 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 510 |
Chain | Residue |
A | ALA347 |
A | GLU348 |
A | ILE349 |
A | THR377 |
A | LYS378 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue DMS A 511 |
Chain | Residue |
A | ARG242 |
A | ILE268 |
A | THR269 |
A | HIS270 |
A | GLN397 |
A | THR398 |
A | PEG503 |
A | HOH605 |
site_id | AD3 |
Number of Residues | 1 |
Details | binding site for residue NA A 512 |
Chain | Residue |
A | GLU348 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:21628583 |
Chain | Residue | Details |
A | TYR126 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor; via carboxylate => ECO:0000305|PubMed:21628583 |
Chain | Residue | Details |
A | PHE402 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22547814, ECO:0000305|PubMed:21628583, ECO:0007744|PDB:3RYO |
Chain | Residue | Details |
A | VAL85 | |
A | SER121 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22547814, ECO:0000305|PubMed:21628583, ECO:0000305|PubMed:24106131, ECO:0000305|PubMed:27010218, ECO:0007744|PDB:3RYO |
Chain | Residue | Details |
A | ARG93 |