3ZU4

Structure of the enoyl-ACP reductase FabV from Yersinia pestis with the cofactor NADH and the 2-pyridone inhibitor PT172

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
A	0006633	biological_process	fatty acid biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0050343	molecular_function	trans-2-enoyl-CoA reductase (NADH) activity
A	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	32
Details	BINDING SITE FOR RESIDUE NAI A 1400

Chain	Residue
A	GLY48
A	GLY110
A	ASP111
A	ALA112
A	PHE113
A	SER138
A	LEU139
A	ALA140
A	PHE223
A	THR224
A	TYR225
A	ALA49
A	LYS244
A	LEU271
A	LYS272
A	ALA273
A	VAL274
A	GLN277
A	ZU41401
A	NA1402
A	HOH2056
A	HOH2101
A	SER50
A	HOH2171
A	HOH2172
A	HOH2236
A	THR51
A	GLY52
A	TYR53
A	PHE73
A	PHE74
A	GLU75

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZU4 A 1401

Chain	Residue
A	ALA140
A	MET196
A	TYR235
A	MET285
A	NAI1400

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site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 1402

Chain	Residue
A	GLY48
A	THR51
A	TYR53
A	GLY54
A	SER138
A	NAI1400

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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_01838, ECO:0000305|PubMed:22244758

Chain	Residue	Details
A	TYR235

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site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:22244758, ECO:0000269|Ref.5

Chain	Residue	Details
A	PHE74
A	ASP111
A	LYS244
A	VAL274
A	GLY48

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01838

Chain	Residue	Details
A	TYR225
A	LEU139

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site_id	SWS_FT_FI4
Number of Residues	1
Details	SITE: Plays an important role in discriminating NADH against NADPH => ECO:0000255|HAMAP-Rule:MF_01838

Chain	Residue	Details
A	GLU75

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