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BioLiP

Structure of PDB 1hwl Chain A

Receptor sequence
>1hwlA (length=407) Species: 9606 (Homo sapiens) [Search protein sequence]
PRPNEECFLSDAEIIQLVNAKHIPAYKLETLIETHERGVSIRRQLLSKKL
SEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGVAGPLCLDEKEFQV
PMATTEGCLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRACDSA
EVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGD
AMGMNMISKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRG
KSVVCEAVIPAKVVREVLKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHA
ANIVTAIYIACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIG
TVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLARIVCGTVMAGELSL
MAALAAG
3D structure
PDB1hwl Structural mechanism for statin inhibition of HMG-CoA reductase.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E559 K691 D767
Catalytic site (residue number reindexed from 1) E106 K238 D314
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 ADP A Y479 N529 Y26 N76
BS02 ADP A A564 N567 R568 K722 A111 N114 R115 K269
BS03 FBI A R590 S684 D690 K691 K692 R137 S231 D237 K238 K239 MOAD: ic50=5nM
BS04 FBI A E559 C561 L562 S565 K735 A751 L853 A856 E106 C108 L109 S112 K282 A298 L400 A403 MOAD: ic50=5nM
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:1hwl, PDBe:1hwl, PDBj:1hwl
PDBsum1hwl
PubMed11349148
UniProtP04035|HMDH_HUMAN 3-hydroxy-3-methylglutaryl-coenzyme A reductase (Gene Name=HMGCR)

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