Structure of PDB 1dub Chain D

Receptor sequence

>1dubD (length=260) Species: 10116 (Rattus norvegicus)

ANFQYIITEKKGKNSSVGLIQLNRPKALNALCNGLIEELNQALETFEEDP
AVGAIVLTGGEKAFAAGADIKEMQNRTFQDCYSGKFLSHWDHITRIKKPV
IAAVNGYALGGGCELAMMCDIIYAGEKAQFGQPEILLGTIPGAGGTQRLT
RAVGKSLAMEMVLTGDRISAQDAKQAGLVSKIFPVETLVEEAIQCAEKIA
NNSKIIVAMAKESVNAAFEMTLTEGNKLEKKLFYSTFATDDRREGMSAFV
EKRKANFKDH

3D structure

• PDB: 1dub Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 angstroms resolution: a spiral fold defines the CoA-binding pocket.
• Chain: D
• Resolution: 2.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): A98 M103 S113 L117 G141 E144 P163 E164 T169 P171 G172 K257 F267
• Catalytic site (residue number reindexed from 1): A68 M73 S83 L87 G111 E114 P133 E134 T139 P141 G142 K227 F237
• Enzyme Commision number: 4.2.1.17: enoyl-CoA hydratase.
  5.3.3.8: Delta(3)-Delta(2)-enoyl-CoA isomerase.

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	CAA	D	F263 F279	F233 F249

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0004165 delta(3)-delta(2)-enoyl-CoA isomerase activity
• GO:0004300 enoyl-CoA hydratase activity
• GO:0016829 lyase activity
• GO:0016836 hydro-lyase activity
• GO:0016853 isomerase activity
• GO:0043956 3-hydroxypropionyl-CoA dehydratase activity
• GO:0120092 crotonyl-CoA hydratase activity

Biological Process

• GO:0006631 fatty acid metabolic process
• GO:0006635 fatty acid beta-oxidation

Cellular Component

• GO:0005739 mitochondrion
• GO:0005759 mitochondrial matrix

External links

• PDB: RCSB:1dub, PDBe:1dub, PDBj:1dub
• PDBsum: 1dub
• PubMed: 8895557
• UniProt: P14604|ECHM_RAT Enoyl-CoA hydratase, mitochondrial (Gene Name=Echs1)