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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
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
A0034054biological_processsymbiont-mediated suppression of host defense-related programmed cell death
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
A0052167biological_processsymbiont-mediated perturbation of host innate immune response
A0061733molecular_functionpeptide-lysine-N-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
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:21628583
ChainResidueDetails
AALA120

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor; via carboxylate => ECO:0000305|PubMed:21628583
ChainResidueDetails
AVAL396

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22547814, ECO:0000305|PubMed:21628583, ECO:0007744|PDB:3RYO
ChainResidueDetails
ATHR79
AVAL115

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:22547814, ECO:0000305|PubMed:21628583, ECO:0000305|PubMed:24106131, ECO:0000305|PubMed:27010218, ECO:0007744|PDB:3RYO
ChainResidueDetails
AVAL87

222415

PDB entries from 2024-07-10

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