BioLiP

Receptor Information

>1dqa Chain D (length=396) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

PAYKLETLIETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYSLVMGAC
CENVIGYMPIPVGVAGPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGLG
GGASSRVLADGMTRGPVVRLPRACDSAEVKAWLETSEGFAVIKEAFDSTS
RFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMISKGTEKALSKLHEYFP
EMQILAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREVLKTTTE
AMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSN
CITLMEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGA
CKDNPGENARQLARIVCGTVMAGELSLMAALAAGHLVKSHMIHNRS

Ligand ID

NAP

InChI

InChI=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

InChIKey

XJLXINKUBYWONI-NNYOXOHSSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 1.5.0	c1cc(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 3.341	NC(=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 3.341	NC(=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 1.5.0	c1cc(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

Formula

C21 H28 N7 O17 P3

Name

NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE;
2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE

PDB chain

1dqa Chain D Residue 4 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	1dqa Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis.
Resolution	2.0 Å
Binding residue (original residue number in PDB)	R590 S626 R627 F628 G652 D653 A654 M655 G656 M657 N658 M659 D690 K691 D767 V805 G807
Binding residue (residue number reindexed from 1)	R114 S150 R151 F152 G176 D177 A178 M179 G180 M181 N182 M183 D214 K215 D291 V329 G331
Annotation score	4

Catalytic site (original residue number in PDB)	E559 K691 D767 H866
Catalytic site (residue number reindexed from 1)	E83 K215 D291 H390
Enzyme Commision number	1.1.1.34: hydroxymethylglutaryl-CoA reductase (NADPH).

	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

PDB	RCSB:1dqa, PDBe:1dqa, PDBj:1dqa
PDBsum	1dqa
PubMed	10698924
UniProt	P04035\|HMDH_HUMAN 3-hydroxy-3-methylglutaryl-coenzyme A reductase (Gene Name=HMGCR)

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Structure of PDB 1dqa Chain D Binding Site BS05