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6VUT

Crystal structure of Eis from Mycobacterium tuberculosis in complex with inhibitor SGT392

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 Residues11
Detailsbinding site for residue RN7 A 501
ChainResidue
AASP26
APEG502
AHOH662
AILE28
AALA33
ATRP36
AMET65
ASER83
APHE84
AGLU401
APHE402

site_idAC2
Number of Residues6
Detailsbinding site for residue PEG A 502
ChainResidue
AHIS119
AALA120
AGLU401
APHE402
ARN7501
AHOH622

site_idAC3
Number of Residues10
Detailsbinding site for residue PEG A 503
ChainResidue
ALEU241
AARG242
AILE267
AILE268
ATHR269
AHIS270
AGLN397
ASO4505
ANA509
AHOH657

site_idAC4
Number of Residues3
Detailsbinding site for residue GOL A 504
ChainResidue
AHIS105
AARG297
AARG353

site_idAC5
Number of Residues8
Detailsbinding site for residue SO4 A 505
ChainResidue
AARG242
AILE268
ATHR269
AHIS270
AGLN397
ATHR398
APEG503
AHOH601

site_idAC6
Number of Residues5
Detailsbinding site for residue SO4 A 506
ChainResidue
ATRP13
AVAL40
APRO41
AALA45
AHOH604

site_idAC7
Number of Residues5
Detailsbinding site for residue SO4 A 507
ChainResidue
AGLY73
AGLY309
ATYR310
ASER392
AASP393

site_idAC8
Number of Residues4
Detailsbinding site for residue NA A 508
ChainResidue
AARG68
ATHR70
AARG183
AGLY189

site_idAC9
Number of Residues6
Detailsbinding site for residue NA A 509
ChainResidue
AHIS249
ATRP253
AILE267
ATHR269
AASP273
APEG503

site_idAD1
Number of Residues6
Detailsbinding site for residue NA A 510
ChainResidue
AGLY130
ALEU296
AARG297
AILE298
AARG353
AGLY357

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

247536

PDB entries from 2026-01-14

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