Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6X10

Crystal structure of acetyltransferase Eis from Mycobacterium tuberculosis in complex with haloperidol

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 Residues8
Detailsbinding site for residue GMJ A 501
ChainResidue
AALA33
AARG37
ALEU63
ASER83
APHE84
AGLU401
APHE402
AHOH682

site_idAC2
Number of Residues4
Detailsbinding site for residue NA A 502
ChainResidue
AGLN185
AVAL394
AHOH886
AGLU74

site_idAC3
Number of Residues2
Detailsbinding site for residue NA A 503
ChainResidue
AGLU401
AHOH703

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL A 504
ChainResidue
AARG37
AVAL40
APRO41
ATHR42
AHOH601
AHOH625
AHOH707

site_idAC5
Number of Residues4
Detailsbinding site for residue GOL A 505
ChainResidue
AHIS105
AARG106
AARG297
AMET299

site_idAC6
Number of Residues6
Detailsbinding site for residue CL A 506
ChainResidue
ATHR269
AGLN397
ATHR398
AHOH736
AHOH782
AHOH811

site_idAC7
Number of Residues2
Detailsbinding site for residue NA A 508
ChainResidue
AALA35
AGLU199

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

237992

PDB entries from 2025-06-25

PDB statisticsPDBj update infoContact PDBjnumon