Structure of PDB 2dub Chain F

Receptor sequence

>2dubF (length=255) Species: 10116 (Rattus norvegicus)

ANFQYIITEKKGKNSSVGLIQLNRPKALNALCNGLIEELNQALETFEEDP
AVGAIVLTGGEKAFAAGADIKEMQNRTFQDCYSHWDHITRIKKPVIAAVN
GYALGGGCELAMMCDIIYAGEKAQFGQPEILLGTIPGAGGTQRLTRAVGK
SLAMEMVLTGDRISAQDAKQAGLVSKIFPVETLVEEAIQCAEKIANNSKI
IVAMAKESVNAAFEMTLTEGNKLEKKLFYSTFATDDRREGMSAFVEKRKA
NFKDH

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: F
• 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): A68 M73 S83 G106 E109 P128 E129 T134 P136 G137 K222 F232
• 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	F	K260 F279 K282	K225 F244 K247
BS02	CO8	F	L58 A96 A98 D99 I100 K101 Y137 G141 E144 P163 E164 L167	L28 A66 A68 D69 I70 K71 Y102 G106 E109 P128 E129 L132

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)