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8VLQ

Structure of PmHMGR bound to mevalonate, CoA and NAD 5 minutes after reaction initiation at pH 9

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0004420molecular_functionhydroxymethylglutaryl-CoA reductase (NADPH) activity
A0015936biological_processcoenzyme A metabolic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0140643molecular_functionhydroxymethylglutaryl-CoA reductase (NADH) activity
B0004420molecular_functionhydroxymethylglutaryl-CoA reductase (NADPH) activity
B0015936biological_processcoenzyme A metabolic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0140643molecular_functionhydroxymethylglutaryl-CoA reductase (NADH) activity
Functional Information from PROSITE/UniProt
site_idPS00066
Number of Residues15
DetailsHMG_COA_REDUCTASE_1 Hydroxymethylglutaryl-coenzyme A reductases signature 1. HlIVdVRDaMGaNtV
ChainResidueDetails
AHIS176-VAL190

site_idPS00318
Number of Residues8
DetailsHMG_COA_REDUCTASE_2 Hydroxymethylglutaryl-coenzyme A reductases signature 2. VGlVGGAT
ChainResidueDetails
AVAL325-THR332

site_idPS01192
Number of Residues14
DetailsHMG_COA_REDUCTASE_3 Hydroxymethylglutaryl-coenzyme A reductases signature 3. ALaTegIqRGHMaL
ChainResidueDetails
AALA371-LEU384

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10003","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1634543","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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