4GGO

Crystal Structure of Trans-2-Enoyl-CoA Reductase from Treponema denticola

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	0016628	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor
A	0050343	molecular_function	trans-2-enoyl-CoA reductase (NADH) activity
A	0051287	molecular_function	NAD binding
B	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
B	0006633	biological_process	fatty acid biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0016628	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor
B	0050343	molecular_function	trans-2-enoyl-CoA reductase (NADH) activity
B	0051287	molecular_function	NAD binding
C	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
C	0006633	biological_process	fatty acid biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0016628	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor
C	0050343	molecular_function	trans-2-enoyl-CoA reductase (NADH) activity
C	0051287	molecular_function	NAD binding
D	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
D	0006633	biological_process	fatty acid biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0016628	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor
D	0050343	molecular_function	trans-2-enoyl-CoA reductase (NADH) activity
D	0051287	molecular_function	NAD binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01838, ECO:0000305|PubMed:22906002, ECO:0000305|PubMed:23050861

Chain	Residue	Details
A	TYR240
B	TYR240
C	TYR240
D	TYR240

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site_id	SWS_FT_FI2
Number of Residues	28
Details	BINDING: BINDING => ECO:0000269|PubMed:23050861

Chain	Residue	Details
A	GLY53
B	ASP116
B	LEU144
B	TYR230
B	LYS249
B	LEU276
C	GLY53
C	PHE79
C	ASP116
C	LEU144
C	TYR230
A	PHE79
C	LYS249
C	LEU276
D	GLY53
D	PHE79
D	ASP116
D	LEU144
D	TYR230
D	LYS249
D	LEU276
A	ASP116
A	LEU144
A	TYR230
A	LYS249
A	LEU276
B	GLY53
B	PHE79

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site_id	SWS_FT_FI3
Number of Residues	4
Details	SITE: Plays an important role in discriminating NADH against NADPH => ECO:0000269|PubMed:23050861

Chain	Residue	Details
A	GLU80
B	GLU80
C	GLU80
D	GLU80

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