3ZU2

Structure of the enoyl-ACP reductase FabV from Yersinia pestis with the cofactor NADH (SIRAS)

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	33
Details	BINDING SITE FOR RESIDUE NAI A 1423

Chain	Residue
A	HIS10
A	GLU98
A	GLY133
A	ASP134
A	ALA135
A	SER161
A	LEU162
A	ALA163
A	SER164
A	PHE246
A	THR247
A	GLY71
A	TYR248
A	LYS267
A	LEU294
A	LYS295
A	ALA296
A	VAL297
A	SER299
A	ALA301
A	SER302
A	NA1424
A	ALA72
A	HOH2057
A	HOH2096
A	HOH2097
A	HOH2121
A	SER73
A	THR74
A	GLY75
A	TYR76
A	PHE96
A	PHE97

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 1424

Chain	Residue
A	GLY71
A	THR74
A	TYR76
A	GLY77
A	SER161
A	NAI1423

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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	TYR258

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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	GLY71
A	PHE97
A	ASP134
A	LYS267
A	VAL297

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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	LEU162
A	TYR248

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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	GLU98

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