8GDN
Structure of PmHMGR bound to mevalonate, CoA and NAD.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004420 | molecular_function | hydroxymethylglutaryl-CoA reductase (NADPH) activity |
A | 0015936 | biological_process | coenzyme A metabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0140643 | molecular_function | hydroxymethylglutaryl-CoA reductase (NADH) activity |
B | 0004420 | molecular_function | hydroxymethylglutaryl-CoA reductase (NADPH) activity |
B | 0015936 | biological_process | coenzyme A metabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0140643 | molecular_function | hydroxymethylglutaryl-CoA reductase (NADH) activity |
Functional Information from PROSITE/UniProt
site_id | PS00066 |
Number of Residues | 15 |
Details | HMG_COA_REDUCTASE_1 Hydroxymethylglutaryl-coenzyme A reductases signature 1. HlIVdVRDaMGaNtV |
Chain | Residue | Details |
A | HIS176-VAL190 |
site_id | PS00318 |
Number of Residues | 8 |
Details | HMG_COA_REDUCTASE_2 Hydroxymethylglutaryl-coenzyme A reductases signature 2. VGlVGGAT |
Chain | Residue | Details |
A | VAL325-THR332 |
site_id | PS01192 |
Number of Residues | 14 |
Details | HMG_COA_REDUCTASE_3 Hydroxymethylglutaryl-coenzyme A reductases signature 3. ALaTegIqRGHMaL |
Chain | Residue | Details |
A | ALA371-LEU384 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: Charge relay system |
Chain | Residue | Details |
A | GLU83 | |
A | LYS267 | |
A | ASP283 | |
B | GLU583 | |
B | LYS767 | |
B | ASP783 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10003, ECO:0000269|PubMed:1634543 |
Chain | Residue | Details |
A | HIS381 | |
B | HIS881 |