Structure of PDB 2dub Chain A Binding Site BS01

Receptor Information
>2dub Chain A (length=254) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NFQYIITEKKGKNSSVGLIQLNRPKALNALCNGLIEELNQALETFEEDPA
VGAIVLTGGEKAFAAGADIKEMQNRTFQDCYSHWDHITRIKKPVIAAVNG
YALGGGCELAMMCDIIYAGEKAQFGQPEILLGTIPGAGGTQRLTRAVGKS
LAMEMVLTGDRISAQDAKQAGLVSKIFPVETLVEEAIQCAEKIANNSKII
VAMAKESVNAAFEMTLTEGNKLEKKLFYSTFATDDRREGMSAFVEKRKAN
FKDH
Ligand information
Ligand IDCO8
InChIInChI=1S/C29H50N7O17P3S/c1-4-5-6-7-8-9-20(38)57-13-12-31-19(37)10-11-32-27(41)24(40)29(2,3)15-50-56(47,48)53-55(45,46)49-14-18-23(52-54(42,43)44)22(39)28(51-18)36-17-35-21-25(30)33-16-34-26(21)36/h16-18,22-24,28,39-40H,4-15H2,1-3H3,(H,31,37)(H,32,41)(H,45,46)(H,47,48)(H2,30,33,34)(H2,42,43,44)/t18-,22-,23-,24+,28-/m1/s1
InChIKeyKQMZYOXOBSXMII-CECATXLMSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CCCCCCCC(=O)SCCNC(=O)CCNC(=O)C(C(C)(C)COP(=O)(O)OP(=O)(O)OCC1C(C(C(O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)O
ACDLabs 10.04O=C(SCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3OP(=O)(O)O)CCCCCCC
OpenEye OEToolkits 1.5.0CCCCCCCC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P@](=O)(O)O[P@](=O)(O)OC[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)O
CACTVS 3.341CCCCCCCC(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)CO[P@@](O)(=O)O[P@@](O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O[P](O)(O)=O)n2cnc3c(N)ncnc23
CACTVS 3.341CCCCCCCC(=O)SCCNC(=O)CCNC(=O)[CH](O)C(C)(C)CO[P](O)(=O)O[P](O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O[P](O)(O)=O)n2cnc3c(N)ncnc23
FormulaC29 H50 N7 O17 P3 S
NameOCTANOYL-COENZYME A
ChEMBL
DrugBankDB02910
ZINCZINC000096014975
PDB chain2dub Chain A Residue 300 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2dub 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.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		K56 A57 L58 A60 A96 A98 D99 I100 K101 G141 E144 P163 E164 G172 A173
Binding residue
(residue number reindexed from 1)		K25 A26 L27 A29 A65 A67 D68 I69 K70 G105 E108 P127 E128 G136 A137
Annotation score3
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.
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

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Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2dub, PDBe:2dub, PDBj:2dub
PDBsum2dub
PubMed9480773
UniProtP14604|ECHM_RAT Enoyl-CoA hydratase, mitochondrial (Gene Name=Echs1)

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