Structure of PDB 1dqa Chain A Binding Site BS05

Receptor Information
>1dqa Chain A (length=409) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LSDAEIIQLVNAKHIPAYKLETLIETHERGVSIRRQLLSKKLSEPSSLQY
LPYRDYNYSLVMGACCENVIGYMPIPVGVAGPLCLDEKEFQVPMATTEGC
LVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRACDSAEVKAWLET
SEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMIS
KGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSVVCEAV
IPAKVVREVLKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIY
IACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIGTVGGGTNL
LPQQACLQMLGVQGACKDNPGENARQLARIVCGTVMAGELSLMAALAAGH
LVKSHMIHN
Ligand information
Ligand IDNAP
InChIInChI=1S/C21H28N7O17P3/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(44-46(33,34)35)14(30)11(43-21)6-41-48(38,39)45-47(36,37)40-5-10-13(29)15(31)20(42-10)27-3-1-2-9(4-27)18(23)32/h1-4,7-8,10-11,13-16,20-21,29-31H,5-6H2,(H7-,22,23,24,25,32,33,34,35,36,37,38,39)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyXJLXINKUBYWONI-NNYOXOHSSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)OP(=O)(O)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[P](O)(O)=O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
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[P](O)(O)=O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]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)OP(=O)(O)O)O)O)O)C(=O)N
FormulaC21 H28 N7 O17 P3
NameNADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE;
2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
ChEMBLCHEMBL295069
DrugBankDB03461
ZINC
PDB chain1dqa Chain B Residue 2 [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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PDB1dqa Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		E559 H866 N870
Binding residue
(residue number reindexed from 1)		E98 H405 N409
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) E559 K691 D767 H866
Catalytic site (residue number reindexed from 1) E98 K230 D306 H405
Enzyme Commision number 1.1.1.34: hydroxymethylglutaryl-CoA reductase (NADPH).
Gene Ontology
Molecular Function
GO:0004420 hydroxymethylglutaryl-CoA reductase (NADPH) activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0050661 NADP binding
Biological Process
GO:0008299 isoprenoid biosynthetic process
GO:0015936 coenzyme A metabolic process
Cellular Component
GO:0005789 endoplasmic reticulum membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1dqa, PDBe:1dqa, PDBj:1dqa
PDBsum1dqa
PubMed10698924
UniProtP04035|HMDH_HUMAN 3-hydroxy-3-methylglutaryl-coenzyme A reductase (Gene Name=HMGCR)

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