Structure of PDB 1dq8 Chain C Binding Site BS01

Receptor Information
>1dq8 Chain C (length=402) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DAEIIQLVNAKHIPAYKLETLIETHERGVSIRRQLLSKKLSEPSSLQYLP
YRDYNYSLVMGACCENVIGYMPIPVGVAGPLCLDEKEFQVPMATTEGCLV
ASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRACDSAEVKAWLETSE
GFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMISKG
TEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIP
AKVVREVLKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIA
CGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIGTVGGGTNLLP
QQACLQMLGVQGACKDNPGENARQLARIVCGTVMAGELSLMAALAAGHLV
KS
Ligand information
Ligand IDCOA
InChIInChI=1S/C21H36N7O16P3S/c1-21(2,16(31)19(32)24-4-3-12(29)23-5-6-48)8-41-47(38,39)44-46(36,37)40-7-11-15(43-45(33,34)35)14(30)20(42-11)28-10-27-13-17(22)25-9-26-18(13)28/h9-11,14-16,20,30-31,48H,3-8H2,1-2H3,(H,23,29)(H,24,32)(H,36,37)(H,38,39)(H2,22,25,26)(H2,33,34,35)/t11-,14-,15-,16+,20-/m1/s1
InChIKeyRGJOEKWQDUBAIZ-IBOSZNHHSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(C)(COP(=O)(O)OP(=O)(O)OCC1C(C(C(O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)C(C(=O)NCCC(=O)NCCS)O
CACTVS 3.341CC(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)[C@@H](O)C(=O)NCCC(=O)NCCS
OpenEye OEToolkits 1.5.0CC(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)[C@H](C(=O)NCCC(=O)NCCS)O
CACTVS 3.341CC(C)(CO[P](O)(=O)O[P](O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O[P](O)(O)=O)n2cnc3c(N)ncnc23)[CH](O)C(=O)NCCC(=O)NCCS
ACDLabs 10.04O=C(NCCS)CCNC(=O)C(O)C(C)(C)COP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3OP(=O)(O)O
FormulaC21 H36 N7 O16 P3 S
NameCOENZYME A
ChEMBLCHEMBL1213327
DrugBankDB01992
ZINCZINC000008551087
PDB chain1dq8 Chain C Residue 102 [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]
PDB1dq8 Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		E559 C561 L562 A564 S565 N567 R568 K722 H752 L853 S865
Binding residue
(residue number reindexed from 1)		E96 C98 L99 A101 S102 N104 R105 K259 H289 L390 S402
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) E559 K691 D767
Catalytic site (residue number reindexed from 1) E96 K228 D304
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1dq8, PDBe:1dq8, PDBj:1dq8
PDBsum1dq8
PubMed10698924
UniProtP04035|HMDH_HUMAN 3-hydroxy-3-methylglutaryl-coenzyme A reductase (Gene Name=HMGCR)

[Back to BioLiP]