Structure of PDB 2dub Chain A

Receptor sequence

>2dubA (length=254) Species: 10116 (Rattus norvegicus)

NFQYIITEKKGKNSSVGLIQLNRPKALNALCNGLIEELNQALETFEEDPA
VGAIVLTGGEKAFAAGADIKEMQNRTFQDCYSHWDHITRIKKPVIAAVNG
YALGGGCELAMMCDIIYAGEKAQFGQPEILLGTIPGAGGTQRLTRAVGKS
LAMEMVLTGDRISAQDAKQAGLVSKIFPVETLVEEAIQCAEKIANNSKII
VAMAKESVNAAFEMTLTEGNKLEKKLFYSTFATDDRREGMSAFVEKRKAN
FKDH

3D structure

• PDB: 2dub The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule.
• Chain: A
• Resolution: 2.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): A98 M103 S113 G141 E144 P163 E164 T169 P171 G172 K257 F267
• Catalytic site (residue number reindexed from 1): A67 M72 S82 G105 E108 P127 E128 T133 P135 G136 K221 F231
• 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	CO8	A	K56 A57 L58 A60 A96 A98 D99 I100 K101 G141 E144 P163 E164 G172 A173	K25 A26 L27 A29 A65 A67 D68 I69 K70 G105 E108 P127 E128 G136 A137

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:2dub, PDBe:2dub, PDBj:2dub
• PDBsum: 2dub
• PubMed: 9480773
• UniProt: P14604|ECHM_RAT Enoyl-CoA hydratase, mitochondrial (Gene Name=Echs1)