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6VUR

Crystal structure of Eis from Mycobacterium tuberculosis in complex with inhibitor SGT366

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 Residues5
Detailsbinding site for residue ROG A 501
ChainResidue
AASP26
ATRP36
ASER83
APHE84
APHE402

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 502
ChainResidue
ATRP13
AARG37
AVAL40
APRO41

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 503
ChainResidue
AGLY73
AGLY309
ATYR310
AASP393

site_idAC4
Number of Residues3
Detailsbinding site for residue GOL A 504
ChainResidue
AARG297
AMET299
AARG353

site_idAC5
Number of Residues8
Detailsbinding site for residue GOL A 505
ChainResidue
APHE24
APHE84
AVAL85
AHIS119
AALA120
ASER121
ATYR126
AHOH740

site_idAC6
Number of Residues8
Detailsbinding site for residue PEG A 506
ChainResidue
ATHR136
APRO271
AGLN272
AALA363
AVAL396
AHOH632
AHOH638
AHOH650

site_idAC7
Number of Residues8
Detailsbinding site for residue PEG A 507
ChainResidue
ALEU241
ATHR269
AHIS270
APRO274
AGLN397
ASO4510
AHOH619
AHOH713

site_idAC8
Number of Residues5
Detailsbinding site for residue NA A 508
ChainResidue
AALA134
ASER358
ALEU361
AGLY362
AALA363

site_idAC9
Number of Residues5
Detailsbinding site for residue NA A 509
ChainResidue
ATHR136
AHIS270
ATHR398
ASO4510
AHOH632

site_idAD1
Number of Residues8
Detailsbinding site for residue SO4 A 510
ChainResidue
AARG242
AILE268
ATHR269
AHIS270
AGLN397
ATHR398
APEG507
ANA509

site_idAD2
Number of Residues5
Detailsbinding site for residue CL A 511
ChainResidue
AARG68
ALEU69
ATHR70
AARG183
AGLY189

site_idAD3
Number of Residues6
Detailsbinding site for residue CL A 512
ChainResidue
AHIS150
AALA153
AHIS277
ALEU278
AALA372
AARG374

site_idAD4
Number of Residues7
Detailsbinding site for residue GOL A 513
ChainResidue
ATHR42
ATYR64
ATYR113
APRO342
ATHR343
AASP344
AHOH625

site_idAD5
Number of Residues3
Detailsbinding site for residue CL A 514
ChainResidue
AGLY95
AARG98
AHOH726

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:21628583
ChainResidueDetails
ATYR126

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor; via carboxylate => ECO:0000305|PubMed:21628583
ChainResidueDetails
APHE402

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22547814, ECO:0000305|PubMed:21628583, ECO:0007744|PDB:3RYO
ChainResidueDetails
AVAL85
ASER121

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
AARG93

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PDB entries from 2024-10-16

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