Structure of PDB 1mj3 Chain F Binding Site BS02

Receptor Information
>1mj3 Chain F (length=258) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ANFQYIITEKKGKNSSVGLIQLNRPKALNALCNGLIEELNQALETFEEDP
AVGAIVLTGGEKAFAAGADIKEMQNRTFQDCYSGLSHWDHITRIKKPVIA
AVNGYALGGGCELAMMCDIIYAGEKAQFGQPEILLGTIPGAGGTQRLTRA
VGKSLAMEMVLTGDRISAQDAKQAGLVSKIFPVETLVEEAIQCAEKIANN
SKIIVAMAKESVNAAFEMTLTEGNKLEKKLFYSTFATDDRREGMSAFVEK
RKANFKDH
Ligand information
Ligand IDHXC
InChIInChI=1S/C27H46N7O17P3S/c1-4-5-6-7-18(36)55-11-10-29-17(35)8-9-30-25(39)22(38)27(2,3)13-48-54(45,46)51-53(43,44)47-12-16-21(50-52(40,41)42)20(37)26(49-16)34-15-33-19-23(28)31-14-32-24(19)34/h14-16,20-22,26,37-38H,4-13H2,1-3H3,(H,29,35)(H,30,39)(H,43,44)(H,45,46)(H2,28,31,32)(H2,40,41,42)/t16-,20-,21-,22+,26-/m1/s1
InChIKeyOEXFMSFODMQEPE-HDRQGHTBSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CCCCCC(=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 3.341CCCCCC(=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
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)CCCCC
CACTVS 3.341CCCCCC(=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
OpenEye OEToolkits 1.5.0CCCCCC(=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
FormulaC27 H46 N7 O17 P3 S
NameHEXANOYL-COENZYME A
ChEMBL
DrugBankDB02563
ZINCZINC000008551760
PDB chain1mj3 Chain F Residue 955 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1mj3 Stereoselectivity of Enoyl-CoA Hydratase Results from Preferential Activation of One of Two Bound Substrate Conformers
Resolution2.1 Å
Binding residue
(original residue number in PDB)		K56 A57 L58 A60 A96 G97 A98 D99 I100 K101 M103 L117 G140 G141 P163 L167
Binding residue
(residue number reindexed from 1)		K26 A27 L28 A30 A66 G67 A68 D69 I70 K71 M73 L85 G108 G109 P131 L135
Annotation score3
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 L85 G109 E112 P131 E132 T137 P139 G140 K225 F235
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
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Cellular Component
External links
PDB RCSB:1mj3, PDBe:1mj3, PDBj:1mj3
PDBsum1mj3
PubMed12445775
UniProtP14604|ECHM_RAT Enoyl-CoA hydratase, mitochondrial (Gene Name=Echs1)

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