Structure of PDB 1f12 Chain A Binding Site BS01

Receptor Information
>1f12 Chain A (length=293) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KIIVKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEES
LRKVAKKKFAENPKAGDECVEKTLSTIATSTDAASVVHSTDLVVEAIVEN
LKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFN
PVPVMKLVEVIKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLL
VPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVGLDTTKFI
VDGWHEMDAENPLHQPSPSLNKLVAENKFGKKTGEGFYKYKLE
Ligand information
Ligand ID3HC
InChIInChI=1S/C25H42N7O18P3S/c1-13(33)8-16(35)54-7-6-27-15(34)4-5-28-23(38)20(37)25(2,3)10-47-53(44,45)50-52(42,43)46-9-14-19(49-51(39,40)41)18(36)24(48-14)32-12-31-17-21(26)29-11-30-22(17)32/h11-14,18-20,24,33,36-37H,4-10H2,1-3H3,(H,27,34)(H,28,38)(H,42,43)(H,44,45)(H2,26,29,30)(H2,39,40,41)/t13-,14+,18+,19+,20-,24+/m0/s1
InChIKeyQHHKKMYHDBRONY-VKBDFPRVSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(CC(=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)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)CC(O)C
OpenEye OEToolkits 1.5.0CC(CC(=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)O
CACTVS 3.341C[C@H](O)CC(=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 3.341C[CH](O)CC(=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
FormulaC25 H42 N7 O18 P3 S
Name3-HYDROXYBUTANOYL-COENZYME A;
3-HYDROXYBUTYRYL-COENZYME A
ChEMBL
DrugBank
ZINCZINC000008551316
PDB chain1f12 Chain A Residue 351 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1f12 Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		K68 S137 H158 F160 N161 M166 N208 L211 P243 M244 L249
Binding residue
(residue number reindexed from 1)		K57 S126 H147 F149 N150 M155 N197 L200 P232 M233 L238
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) S137 H158 E170 N208
Catalytic site (residue number reindexed from 1) S126 H147 E159 N197
Enzyme Commision number 1.1.1.35: 3-hydroxyacyl-CoA dehydrogenase.
Gene Ontology
Molecular Function
GO:0003857 3-hydroxyacyl-CoA dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0016740 transferase activity
GO:0042802 identical protein binding
GO:0070403 NAD+ binding
Biological Process
GO:0006631 fatty acid metabolic process
GO:0006635 fatty acid beta-oxidation
GO:0007283 spermatogenesis
GO:0009410 response to xenobiotic stimulus
GO:0009725 response to hormone
GO:0014823 response to activity
GO:0030154 cell differentiation
GO:0032868 response to insulin
GO:0046676 negative regulation of insulin secretion
GO:0050796 regulation of insulin secretion
GO:0120162 positive regulation of cold-induced thermogenesis
Cellular Component
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1f12, PDBe:1f12, PDBj:1f12
PDBsum1f12
PubMed10840044
UniProtQ16836|HCDH_HUMAN Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial (Gene Name=HADH)

[Back to BioLiP]