6VUY

Crystal structure of Eis from Mycobacterium tuberculosis in complex with inhibitor SGT358

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0005829	cellular_component	cytosol
A	0008080	molecular_function	N-acetyltransferase activity
A	0016746	molecular_function	acyltransferase activity
A	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
A	0030649	biological_process	aminoglycoside antibiotic catabolic process
A	0033661	biological_process	effector-mediated defense to host-produced reactive oxygen species
A	0034054	biological_process	symbiont-mediated suppression of host defense-related programmed cell death
A	0034069	molecular_function	aminoglycoside N-acetyltransferase activity
A	0042802	molecular_function	identical protein binding
A	0043655	cellular_component	host extracellular space
A	0044161	cellular_component	host cell cytoplasmic vesicle
A	0046677	biological_process	response to antibiotic
A	0051701	biological_process	biological process involved in interaction with host
A	0052032	biological_process	symbiont-mediated perturbation of host inflammatory response
A	0052040	biological_process	symbiont-mediated perturbation of host programmed cell death
A	0052167	biological_process	symbiont-mediated perturbation of host innate immune response
A	0061733	molecular_function	peptide-lysine-N-acetyltransferase activity
A	0097691	cellular_component	bacterial extracellular vesicle

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	binding site for residue RN4 A 501

Chain	Residue
A	TRP13
A	TRP36
A	ARG37
A	MET65
A	SER83
A	PHE84
A	GLU401
A	PHE402
A	HOH717

---

site_id	AC2
Number of Residues	7
Details	binding site for residue PEG A 502

Chain	Residue
A	LEU241
A	HIS249
A	ILE267
A	THR269
A	HIS270
A	GLN397
A	HOH620

---

site_id	AC3
Number of Residues	4
Details	binding site for residue PEG A 503

Chain	Residue
A	THR38
A	ASP66
A	THR343
A	ASP344

---

site_id	AC4
Number of Residues	3
Details	binding site for residue DMS A 504

Chain	Residue
A	GLU348
A	GLU350
A	LYS378

---

site_id	AC5
Number of Residues	5
Details	binding site for residue GOL A 507

Chain	Residue
A	GLU139
A	THR141
A	ARG237
A	ARG264
A	HOH688

---

site_id	AC6
Number of Residues	5
Details	binding site for residue GOL A 508

Chain	Residue
A	ARG192
A	LEU196
A	GLU199
A	GLU203
A	HOH602

---

site_id	AC7
Number of Residues	4
Details	binding site for residue NA A 509

Chain	Residue
A	GLY123
A	THR280
A	THR282
A	TRP295

---

site_id	AC8
Number of Residues	3
Details	binding site for residue NA A 510

Chain	Residue
A	SER214
A	ARG227
A	SER239

---

site_id	AC9
Number of Residues	3
Details	binding site for residue NA A 511

Chain	Residue
A	GLY315
A	GLU316
A	ARG385

---

site_id	AD1
Number of Residues	3
Details	binding site for residue NA A 512

Chain	Residue
A	GLU213
A	SER214
A	PHE215

---

site_id	AD2
Number of Residues	5
Details	binding site for residue MG A 513

Chain	Residue
A	ALA134
A	SER358
A	LEU361
A	GLY362
A	ALA363

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000305|PubMed:21628583

Chain	Residue	Details
A	TYR126

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton acceptor; via carboxylate => ECO:0000305|PubMed:21628583

Chain	Residue	Details
A	PHE402

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:22547814, ECO:0000305|PubMed:21628583, ECO:0007744|PDB:3RYO

Chain	Residue	Details
A	VAL85
A	SER121

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:22547814, ECO:0000305|PubMed:21628583, ECO:0000305|PubMed:24106131, ECO:0000305|PubMed:27010218, ECO:0007744|PDB:3RYO

Chain	Residue	Details
A	ARG93

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