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5EBV

Crystal structure of acetyltransferase Eis from Mycobacterium tuberculosis in complex with inhibitor 11c and CoA

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0005829cellular_componentcytosol
A0008080molecular_functionN-acetyltransferase activity
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0030649biological_processaminoglycoside antibiotic catabolic process
A0033661biological_processeffector-mediated defense to host-produced reactive oxygen species
A0034069molecular_functionaminoglycoside N-acetyltransferase activity
A0042802molecular_functionidentical protein binding
A0043655cellular_componenthost extracellular space
A0044161cellular_componenthost cell cytoplasmic vesicle
A0046677biological_processresponse to antibiotic
A0051701biological_processbiological process involved in interaction with host
A0052032biological_processsymbiont-mediated perturbation of host inflammatory response
A0052040biological_processsymbiont-mediated perturbation of host programmed cell death
A0052041biological_processsymbiont-mediated suppression of host programmed cell death
A0052167biological_processsymbiont-mediated perturbation of host innate immune response
A0061733molecular_functionprotein-lysine-acetyltransferase activity
A0097691cellular_componentbacterial extracellular vesicle
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue COA A 501
ChainResidue
AVAL87
ATYR126
AASP260
AHOH646
AARG92
AARG93
AARG94
AGLY95
ALEU96
ALEU97
AARG98
AILE125

site_idAC2
Number of Residues13
Detailsbinding site for residue 5LR A 502
ChainResidue
APHE24
AASP26
APHE27
AALA33
ATRP36
AARG37
ASER83
APHE84
AVAL85
AHIS119
AGLU401
APHE402
AHOH623

site_idAC3
Number of Residues2
Detailsbinding site for residue CL A 503
ChainResidue
ATHR269
ATHR398

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"21628583","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor; via carboxylate","evidences":[{"source":"PubMed","id":"21628583","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22547814","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21628583","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3RYO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues5
DetailsBinding 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"}]}
ChainResidueDetails

244349

PDB entries from 2025-11-05

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