3ZU3

Structure of the enoyl-ACP reductase FabV from Yersinia pestis with the cofactor NADH (MR, cleaved Histag)

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	37
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	SER141
A	PHE223
A	THR224
A	ALA49
A	TYR225
A	LYS244
A	LYS272
A	ALA273
A	VAL274
A	SER276
A	ALA278
A	SER279
A	NA1405
A	HOH2105
A	SER50
A	HOH2108
A	HOH2192
A	HOH2197
A	HOH2199
A	HOH2269
A	HOH2304
A	HOH2308
A	HOH2419
A	THR51
A	GLY52
A	TYR53
A	PHE73
A	PHE74
A	GLU75

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 1401

Chain	Residue
A	ASP172
A	GLU303
A	SER311
A	TYR334
A	LYS335
A	HOH2298
A	HOH2420
A	HOH2421

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 1402

Chain	Residue
A	ASP111
A	PHE113
A	ARG143
A	ARG144
A	THR145
A	HOH2201
A	HOH2422

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1403

Chain	Residue
A	GLU79
A	GLU80
A	LYS106
A	ASP390
A	ASN395
A	ILE397

---

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 1404

Chain	Residue
A	PRO77
A	TRP88
A	ASP390
A	LYS392
A	HOH2412
A	HOH2416
A	HOH2423

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA A 1405

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

---

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

---

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

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

---

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

Chain	Residue	Details
A	LEU139
A	TYR225

---

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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