5IV0

Crystal structure of Eis from Mycobacterium tuberculosis in complex with sulfonamide inhibitor 39 and coenzyme A

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	0016740	molecular_function	transferase 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	16
Details	binding site for residue COA A 501

Chain	Residue
A	VAL85
A	HIS119
A	ILE125
A	TYR126
A	ASP260
A	6E9502
A	HOH635
A	HOH674
A	VAL87
A	ARG92
A	ARG93
A	ARG94
A	GLY95
A	LEU96
A	LEU97
A	ARG98

---

site_id	AC2
Number of Residues	11
Details	binding site for residue 6E9 A 502

Chain	Residue
A	PHE24
A	ASP26
A	PHE27
A	ILE28
A	ALA33
A	TRP36
A	SER83
A	PHE84
A	SER121
A	PHE402
A	COA501

---

site_id	AC3
Number of Residues	5
Details	binding site for residue CL A 503

Chain	Residue
A	ARG68
A	LEU69
A	THR70
A	ARG183
A	GLY189

---

site_id	AC4
Number of Residues	2
Details	binding site for residue CL A 504

Chain	Residue
A	THR269
A	THR398

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01812

Chain	Residue	Details
A	ALA120

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton acceptor; via carboxylate => ECO:0000255|HAMAP-Rule:MF_01812

Chain	Residue	Details
A	VAL396

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01812

Chain	Residue	Details
A	THR79
A	VAL87
A	VAL115

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000305|PubMed:21628583

Chain	Residue	Details
A	TYR126

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	ACT_SITE: Proton acceptor; via carboxylate => ECO:0000305|PubMed:21628583

Chain	Residue	Details
A	PHE402

---

site_id	SWS_FT_FI6
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_FI7
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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