Structure of PDB 1qay Chain B

Receptor sequence
>1qayB (length=374) Species: 32044 (Pseudomonas sp. 'mevalonii') [Search protein sequence]
DSRLPAFRNLSPAARLDHIGQLLGLSHDDVSLLANAGALPMDIANGMIEN
VIGTFELPYAVASNFQINGRDVLVPLVVEEPSIVAAASYMAKLARANGGF
TTSSSAPLMHAQVQIVGIQDPLNARLSLLRRKDEIIELANRKDQLLNSLG
GGCRDIEVHTFADTPRGPMLVAHLIVDVRDAMGANTVNTMAEAVAPLMEA
ITGGQVRLRILSNLADLRLARAQVRITPQQLETAEFSGEAVIEGILDAYA
FAAVDPYRAATHNKGIMNGIDPLIVATGNDWRAVEAGAHAYACRSGHYGS
LTTWEKDNNGHLVGTLEMPMPVGLVGGATKTHPLAQLSLRILGVKTAQAL
AEIAVAVGLAQNLGAMRALATEGI
3D structure
PDB1qay Substrate-induced closure of the flap domain in the ternary complex structures provides insights into the mechanism of catalysis by 3-hydroxy-3-methylglutaryl-CoA reductase.
ChainB
Resolution2.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.1.1.88: hydroxymethylglutaryl-CoA reductase.
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 NAD B L652 R682 D683 A684 G686 A687 N688 T689 L714 N716 V828 L149 R179 D180 A181 G183 A184 N185 T186 L211 N213 V325
Gene Ontology
Molecular Function
GO:0004420 hydroxymethylglutaryl-CoA reductase (NADPH) activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0140643 hydroxymethylglutaryl-CoA reductase (NADH) activity
Biological Process
GO:0015936 coenzyme A metabolic process

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Molecular Function

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Biological Process
External links
PDB RCSB:1qay, PDBe:1qay, PDBj:1qay
PDBsum1qay
PubMed10377386
UniProtP13702|MVAA_PSEMV 3-hydroxy-3-methylglutaryl-coenzyme A reductase (Gene Name=mvaA)

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