Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4FW5

Crystal Structure of the LpxC in complex with 4'-BROMO-N-[(2S,3R)-3-HYDROXY-1-(HYDROXYAMINO)-1-OXOBUTAN-2-YL]BIPHENYL-4-CARBOXAMIDE inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006796	biological_process	phosphate-containing compound metabolic process
A	0008759	molecular_function	UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity
A	0009245	biological_process	lipid A biosynthetic process
A	0016787	molecular_function	hydrolase activity
A	0019637	biological_process	organophosphate metabolic process
A	0046872	molecular_function	metal ion binding
A	0103117	molecular_function	UDP-3-O-acyl-N-acetylglucosamine deacetylase activity
A	1901135	biological_process	carbohydrate derivative metabolic process
B	0006796	biological_process	phosphate-containing compound metabolic process
B	0008759	molecular_function	UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity
B	0009245	biological_process	lipid A biosynthetic process
B	0016787	molecular_function	hydrolase activity
B	0019637	biological_process	organophosphate metabolic process
B	0046872	molecular_function	metal ion binding
B	0103117	molecular_function	UDP-3-O-acyl-N-acetylglucosamine deacetylase activity
B	1901135	biological_process	carbohydrate derivative metabolic process
C	0006796	biological_process	phosphate-containing compound metabolic process
C	0008759	molecular_function	UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity
C	0009245	biological_process	lipid A biosynthetic process
C	0016787	molecular_function	hydrolase activity
C	0019637	biological_process	organophosphate metabolic process
C	0046872	molecular_function	metal ion binding
C	0103117	molecular_function	UDP-3-O-acyl-N-acetylglucosamine deacetylase activity
C	1901135	biological_process	carbohydrate derivative metabolic process
D	0006796	biological_process	phosphate-containing compound metabolic process
D	0008759	molecular_function	UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity
D	0009245	biological_process	lipid A biosynthetic process
D	0016787	molecular_function	hydrolase activity
D	0019637	biological_process	organophosphate metabolic process
D	0046872	molecular_function	metal ion binding
D	0103117	molecular_function	UDP-3-O-acyl-N-acetylglucosamine deacetylase activity
D	1901135	biological_process	carbohydrate derivative metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 301

Chain	Residue
A	HIS78
A	HIS237
A	ASP241
A	L58302

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE L58 A 302

Chain	Residue
A	ILE197
A	ARG201
A	GLY209
A	SER210
A	ALA214
A	HIS237
A	LYS238
A	ASP241
A	HIS264
A	ZN301
A	HOH452
A	MET62
A	GLU77
A	HIS78
A	THR190
A	PHE191

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT A 303

Chain	Residue
A	ARG143
A	ARG258
A	GLY259
A	PHE260
A	HOH536

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 304

Chain	Residue
A	PHE152
A	ILE243
A	LEU246
A	TYR247
A	SER252
A	LEU253
A	HOH479
A	HOH500
A	HOH520

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 301

Chain	Residue
B	HIS78
B	HIS237
B	ASP241
B	L58302

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE L58 B 302

Chain	Residue
B	MET62
B	GLU77
B	HIS78
B	THR190
B	PHE191
B	ILE197
B	GLY209
B	ALA214
B	VAL216
B	HIS237
B	LYS238
B	ASP241
B	HIS264
B	ZN301

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT B 303

Chain	Residue
B	ARG143
B	ARG258
B	PHE260
B	HOH539

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT B 304

Chain	Residue
B	SER40
B	GLU49
B	TYR92
B	GLU94

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT B 305

Chain	Residue
B	GLY85
B	PHE176
B	SER295
B	HOH458

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 306

Chain	Residue
B	PHE152
B	ILE243
B	LEU246
B	TYR247
B	SER252
B	LEU253
B	HOH424

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 301

Chain	Residue
C	HIS78
C	HIS237
C	ASP241
C	L58302

site_id	BC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE L58 C 302

Chain	Residue
C	MET62
C	GLU77
C	HIS78
C	THR190
C	PHE191
C	GLY192
C	GLY209
C	SER210
C	ALA214
C	VAL216
C	HIS237
C	LYS238
C	ASP241
C	HIS264
C	ZN301

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT C 303

Chain	Residue
C	PRO46
C	VAL47
C	HOH454

site_id	BC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL C 304

Chain	Residue
C	HOH426
C	HOH453
C	HOH467
C	PHE152
C	ILE243
C	LEU246
C	TYR247
C	SER252
C	LEU253

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 301

Chain	Residue
D	HIS78
D	HIS237
D	ASP241
D	L58302

site_id	BC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE L58 D 302

Chain	Residue
D	MET62
D	GLU77
D	HIS78
D	THR190
D	PHE191
D	MET194
D	GLY209
D	SER210
D	VAL216
D	HIS237
D	LYS238
D	ASP241
D	HIS264
D	ZN301

site_id	BC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL D 303

Chain	Residue
D	PHE152
D	ILE243
D	LEU246
D	TYR247
D	SER252
D	LEU253
D	HOH488
D	HOH496
D	HOH511

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000255\|HAMAP-Rule:MF_00388

Chain	Residue	Details
A	HIS264
B	HIS264
C	HIS264
D	HIS264

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00388

Chain	Residue	Details
A	HIS78
D	HIS78
D	HIS237
D	ASP241
A	HIS237
A	ASP241
B	HIS78
B	HIS237
B	ASP241
C	HIS78
C	HIS237
C	ASP241

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)