Structure of PDB 4eue Chain A

Receptor sequence

>4eueA (length=398) Species: 272562 (Clostridium acetobutylicum ATCC 824)

MIVKAKFVKGFIRDVHPYGCRREVLNQIDYCKKAIGFRGPKKVLIVGASS
GFGLATRISVAFGGPEAHTIGVSYETGATDRRIGTAGWYNNIFFKEFAKK
KGLVAKNFIEDAFSNETKDKVIKYIKDEFGKIDLFVYSLAAPRRKDYKTG
NVYTSRIKTILGDFEGPTIDVERDEITLKKVSSASIEEIEETRKVMGGED
WQEWCEELLYEDCFSDKATTIAYSYIGSPRTYKIYREGTIGIAKKDLEDK
AKLINEKLNRVIGGRAFVSVNKALVTKASAYIPTFPLYAAILYKVMKEKN
IHENCIMQIERMFSEKIYSNEKIQFDDKGRLRMDDLELRKDVQDEVDRIW
SNITPENFKELSDYKGYKKEFMNLNGFDLDGVDYSKDLDIELLRKLEP

3D structure

• PDB: 4eue Structures of trans-2-enoyl-CoA reductases from Clostridium acetobutylicum and Treponema denticola: insights into the substrate specificity and the catalytic mechanism
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• Enzyme Commision number: 1.3.1.44: trans-2-enoyl-CoA reductase (NAD(+)).

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	NAI	A	G47 S49 S50 G51 F52 S73 Y74 E75 E110 D111 A112 S138 L139 A140 S224 K244 L274 T276 A278 S279	G47 S49 S50 G51 F52 S73 Y74 E75 E110 D111 A112 S138 L139 A140 S224 K244 L274 T276 A278 S279

Gene Ontology

Molecular Function

• GO:0004318 enoyl-[acyl-carrier-protein] reductase (NADH) activity
• GO:0016491 oxidoreductase activity
• GO:0016628 oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor
• GO:0050343 trans-2-enoyl-CoA reductase (NADH) activity
• GO:0051287 NAD binding

Biological Process

• GO:0006633 fatty acid biosynthetic process

External links

• PDB: RCSB:4eue, PDBe:4eue, PDBj:4eue
• PDBsum: 4eue
• PubMed: 23050861
• UniProt: Q97LU2|FABV_CLOAB Trans-2-enoyl-CoA reductase [NADH] (Gene Name=fabV)