Structure of PDB 1m76 Chain B Binding Site BS02

Receptor Information
>1m76 Chain B (length=291) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KIIVKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEES
LRKVAKKKFAENPKAGDEFVEKTLSTIATSTDAASVVHSTDLVVEAIVEN
LKVKNELFKRLDKFAAEHTIFASNTCSLQITSIANATTRQDRFAGLHFFN
PVPVMKLVEVIKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLL
VPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVGLDTTKFI
VDGWHEMDAENPLHQPSPSLNKLVAENKFGKKTGEGFYKYK
Ligand information
Ligand IDNAD
InChIInChI=1S/C21H27N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1-4,7-8,10-11,13-16,20-21,29-32H,5-6H2,(H5-,22,23,24,25,33,34,35,36,37)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyBAWFJGJZGIEFAR-NNYOXOHSSA-N
SMILES
SoftwareSMILES
CACTVS 3.341NC(=O)c1ccc[n+](c1)[C@@H]2O[C@H](CO[P]([O-])(=O)O[P@](O)(=O)OC[C@H]3O[C@H]([C@H](O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)N
CACTVS 3.341NC(=O)c1ccc[n+](c1)[CH]2O[CH](CO[P]([O-])(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)([O-])O[P@@](=O)(O)OC[C@@H]3[C@H]([C@H]([C@@H](O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)N
FormulaC21 H27 N7 O14 P2
NameNICOTINAMIDE-ADENINE-DINUCLEOTIDE
ChEMBLCHEMBL1234613
DrugBankDB14128
ZINC
PDB chain1m76 Chain B Residue 750 [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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PDB1m76 Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxyacyl-COA dehydrogenase provide insights into catalytic mechanism
Resolution2.15 Å
Binding residue
(original residue number in PDB)		G24 L25 M26 D45 Q46 A107 I108 E110 K115 N135 C137 H158 N161 V253 K293
Binding residue
(residue number reindexed from 1)		G13 L14 M15 D34 Q35 A96 I97 E99 K104 N124 C126 H147 N150 V242 K282
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) C137 H158 E170 N208
Catalytic site (residue number reindexed from 1) C126 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:1m76, PDBe:1m76, PDBj:1m76
PDBsum1m76
PubMed
UniProtQ16836|HCDH_HUMAN Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial (Gene Name=HADH)

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