Structure of PDB 1dq9 Chain C

Receptor sequence

>1dq9C (length=407) Species: 9606 (Homo sapiens)

KFLSDAEIIQLVNAKHIPAYKLETLIETHERGVSIRRQLLSKKLSEPSSL
QYLPYRDYNYSLVMGACCENVIGYMPIPVGVAGPLCLDEKEFQVPMATTE
GCLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRACDSAEVKAWL
ETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNM
ISKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSVVCE
AVIPAKVVREVLKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTA
IYIACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIGTVGGGT
NLLPQQACLQMLGVQGACKDNPGENARQLARIVCGTVMAGELSLMAALAA
GHLVKSH

3D structure

• PDB: 1dq9 Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis.
• Chain: C
• Resolution: 2.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): E559 K691 D767 H866
• Catalytic site (residue number reindexed from 1): E100 K232 D308 H407
• Enzyme Commision number: 1.1.1.34: hydroxymethylglutaryl-CoA reductase (NADPH).

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	HMG	C	E559 A564 S565 N567 R568 K722 K735 L853 A856 L862 S865 H866	E100 A105 S106 N108 R109 K263 K276 L394 A397 L403 S406 H407
BS02	HMG	C	Y479 R590 S684 D690 K692	Y20 R131 S225 D231 K233

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

External links

• PDB: RCSB:1dq9, PDBe:1dq9, PDBj:1dq9
• PDBsum: 1dq9
• PubMed: 10698924
• UniProt: P04035|HMDH_HUMAN 3-hydroxy-3-methylglutaryl-coenzyme A reductase (Gene Name=HMGCR)