Structure of PDB 1qax Chain A

Receptor sequence
>1qaxA (length=425) Species: 32044 (Pseudomonas sp. 'mevalonii') [Search protein sequence]
DSRLPAFRNLSPAARLDHIGQLLGLSHDDVSLLANAGALPMDIANGMIEN
VIGTFELPYAVASNFQINGRDVLVPLVVEEPSIVAAASYMAKLARANGGF
TTSSSAPLMHAQVQIVGIQDPLNARLSLLRRKDEIIELANRKDQLLNSLG
GGCRDIEVHTFADTPRGPMLVAHLIVDVRDAMGANTVNTMAEAVAPLMEA
ITGGQVRLRILSNLADLRLARAQVRITPQQLETAEFSGEAVIEGILDAYA
FAAVDPYRAATHNKGIMNGIDPLIVATGNDWRAVEAGAHAYACRSGHYGS
LTTWEKDNNGHLVGTLEMPMPVGLVGGATKTHPLAQLSLRILGVKTAQAL
AEIAVAVGLAQNLGAMRALATEGIQRGHMALHARNIAVVAGARGDEVDWV
ARQLVEYHDVRADRAVALLKQKRGQ
3D structure
PDB1qax 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.
ChainA
Resolution2.8 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 HMG A R11 E83 A88 Y92 K95 R261 T264 G268 N271 Q364 A368 L372 R8 E80 A85 Y89 K92 R258 T261 G265 N268 Q361 A365 L369
BS02 NAD A E83 K267 A415 E80 K264 A412
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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1qax, PDBe:1qax, PDBj:1qax
PDBsum1qax
PubMed10377386
UniProtP13702|MVAA_PSEMV 3-hydroxy-3-methylglutaryl-coenzyme A reductase (Gene Name=mvaA)

[Back to BioLiP]