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3-hydroxy-3-methylglutaryl coenzyme A reductase [Q9Y0F3]
Systematic NameLmjF.30.3190 [Leishmania major]
Gene NameHMGR
Molecular Weight45953 Da
Protein Sequence Size434
Function
Charge11.5
Isoelectric Point8.3 pH
Description3-hydroxy-3-methylglutaryl coenzyme A reductase (3-hydroxy-3- methylglutaryl-CoA reductase, putative).
Subcellular Locationintegral to membrane; Mitochondrion[Predict]
E. C. Number N.A.
Sequence>tr|Q9Y0F3|Q9Y0F3_LEIMA 3-hydroxy-3-methylglutaryl coenzyme A reductase (3-hydroxy-3- methylglutaryl-CoA reductase, putative) - Leishmania major.
RRSLLLACSAAKGESWASMSDTEIMKQVENKKIAFHGLEQALAPDYDRAIAIRREIVKKK
ICPSPAATHPLERVPYKNYDWSSVVGQSCENILGYVPVPVGLAGPLLLDGKEVALPMATT
EGALVASAHRGARAINLSGGCRTAVLKEGMTRAPVVEVNSFDEAITVIKFCEERFDVLRE
AFESTTRFGKLLSIKCAMAGRQVHLRFSAFTGDAMGMNMITKGCDKALQVLQQHIPSVRV
LTLSGNFCTDKKPSALNWVEGRGKSVVAEAVIKRDVVESVLKCTVDSVVSLNVTKNLRGS
ALAGSIGGFNAHAANIVAALYIATGQDPAQVVESATCMTTVDKAGEDLVISLMMPSIEVG
AVGGGTGLSSQRAMLELMGCAGSNKEDPGAHSRQIARVVAGAVICGELSLLSGLAAGHLL
SAHMKLNRKPPTP
DNA Sequence>LmjF30.3190 |HMGR||3-hydroxy-3-methylglutaryl-CoA reductase, putative|Leishmania major|chr 30|||Manual
ATGCGCCGCT CTCTGCTGCT TGCCTGCTCC GCCGCCAAGG GTGAGAGCTG GGCATCCATGTCCGATACAG AGATCATGAA GCAGGTGGAG AATAAGAAGA TTGCATTTCA CGGCCTTGAGCAGGCTCTTG CACCCGACTA TGACCGCGCC ATCGCCATTC GTCGTGAGAT TGTGAAGAAAAAGATATGTC CATCTCCAGC TGCCACACAT CCGCTGGAGA GGGTTCCCTA CAAGAACTACGACTGGAGCA GTGTTGTGGG ACAGAGCTGC GAGAACATCC TCGGCTACGT TCCGGTACCGGTAGGGTTGG CTGGTCCGCT GCTGTTGGAT GGAAAGGAAG TGGCACTGCC GATGGCGACGACGGAGGGTG CGCTGGTCGC GAGTGCGCAC CGCGGTGCTC GCGCCATCAA CCTGAGCGGCGGATGCCGGA CAGCGGTGCT GAAGGAAGGC ATGACGCGCG CCCCTGTAGT GGAGGTGAACTCCTTCGACG AGGCCATCAC CGTGATCAAG TTCTGTGAGG AGCGGTTCGA CGTTCTAAGGGAGGCCTTCG AGTCGACGAC CCGCTTCGGG AAGTTGCTGA GCATCAAGTG TGCCATGGCGGGTCGCCAGG TGCATCTGCG CTTCTCTGCC TTTACCGGAG ATGCGATGGG CATGAATATGATCACGAAGG GCTGCGACAA GGCGCTGCAG GTGCTGCAGC AGCACATTCC CTCTGTGCGAGTGCTGACCT TGTCAGGCAA CTTCTGCACT GACAAGAAAC CGTCCGCACT GAACTGGGTGGAGGGACGCG GGAAGTCGGT CGTAGCGGAG GCCGTCATCA AGCGTGATGT GGTCGAGAGTGTTCTCAAGT GCACGGTGGA CAGTGTTGTG TCGCTGAATG TAACTAAGAA CCTGCGCGGATCTGCGCTTG CCGGTTCCAT CGGCGGCTTC AACGCACACG CTGCCAACAT CGTGGCCGCGCTCTACATCG CCACTGGCCA GGACCCCGCA CAGGTAGTGG AGTCCGCAAC CTGCATGACGACGGTTGACA AGGCTGGTGA GGATCTCGTG ATCAGCCTCA TGATGCCGAG CATTGAGGTCGGCGCCGTAG GCGGTGGTAC AGGTCTGTCG TCGCAGCGCG CCATGCTGGA GCTGATGGGGTGCGCGGGCT CTAACAAGGA GGACCCAGGT GCCCACTCCC GCCAGATCGC GCGTGTCGTTGCTGGCGCAG TCATTTGCGG TGAGCTGTCC CTCTTGTCCG GCCTTGCAGC TGGCCACTTACTAAGCGCCC ACATGAAGCT GAACCGCAAG CCTCCGACTC CGTAA
3-hydroxy-3-methylglutaryl coenzyme A reductase Q9Y0F3]
Metabolite Information
Molecular Functionhydroxymethylglutaryl-CoA reductase (NADPH) activity
Biochemical Pathwaybiosynthesis; isoprenoid biosynthesis; lipid metabolism
Regulatory Pathway
KEGG PathwaysK00021
Orthologs
Homologs GI Percent Identity Evalue Score
Homo sapiens3-hydroxy-3-methylglutaryl-Coenzyme A reductase [Homo sapiens]481e-101367
DEG Information
DEG Protein DEG Organism Percent Identity Evalue Bit Score
3-hydroxy-3-methylglutaryl-CoA reductaseStreptococcus pneumoniae19%0.00238.1
Post Translational Modification
PTM Type PTM Sub Type Score Modification Site Prosite ID
PDOC00064Hydroxymethylglutaryl-coenzyme A reductase signatures and profile207-221; PS00066
PDOC00064Hydroxymethylglutaryl-coenzyme A reductase signatures and profile360-367; PS00318
PDOC00064Hydroxymethylglutaryl-coenzyme A reductase signatures and profile107.55722-429PS50065
AcylationN-myristoylation site38-43; 123-128; 140-145; 141-146; 224-229; 246-251; 300-305; 305-310; 308-313; 326-331; 361-366; 364-369; 366-371; 380-385; 402-407; 414-419; PS00008
GlycosylationN-glycosylation site137-140; 293-296; PS00001
PhosphorylationcAMP- and cGMP-dependent protein kinase phosphorylation site252-255; PS00004
PhosphorylationCasein kinase II phosphorylation site19-22; 21-24; 161-164; 325-328; 340-343; 384-387; PS00006
PhosphorylationProtein kinase C phosphorylation site186-188; 194-196; 238-240; 250-252; 371-373; 384-386; PS00005
3-hydroxy-3-methylglutaryl coenzyme A reductase [Q9Y0F3]
Model Information
Template PDB ID2q6cD
Percent Identity48%
Target Region7-425
Template Region442-861
Domain Information
Domains Start End
Active Site Information
Residue Active Site Number Functional Part
GLU116Unknown
LYS246Unknown
ASP322Unknown
Co-Factor
Metal Description
Ligands
CAS number Name Mol. Weight Mol. Formula Smile Notation PDB Reference
(3R,5R)-7-[1-(4-FLUOROPHENYL)-3-ISOPROPYL- 4-OXO-5-PHENYL-4,5-DIHYDRO-3H-PYRROLO[2,3- C]QUINOLIN-2-YL]-3,5-DIHYDROXYHEPTANOIC ACID556.624C33 H33 F N2 O5O=C(O)CC(O)CC(O)CCc3c(c2c1c(cccc1)N(C(=O)c2n3C(C)C)c4ccccc4)c5ccc(F)cc52q6c
14808-79-8SULFATE ION96.063O4 S  [O-]S([O-])(=O)=O 2q6c
Mutational Information
Residue Feature Description
Modeled Protein Template Structure
+----------<<< P R O C H E C K S U M = M A R Y >>>----------+ | = | | /var/www/html/Services/SAVES_3/jobs/1786065/Q9Y0F3.pdb 2.0 413 = residues | | = | +| Ramachandran plot: 93.6% core 5.6% allow 0.8% gener 0.0% = disall | | = | +| All Ramachandrans: 10 labelled residues (out of 411) = | +| Chi1-chi2 plots: 1 labelled residues (out of 204) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | *| Residue properties: Max.deviation: 2.7 Bad contacts: = 5 | *| Bond len/angle: 8.0 Morris et al class: 1 = 1 2 | +| 2 cis-peptides = | | G-factors Dihedrals: 0.06 Covalent: -0.13 Overall: = -0.01 | | = | | M/c bond lengths: 99.3% within limits 0.7% highlighted = | | M/c bond angles: 94.1% within limits 5.9% highlighted = | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further.
Overlapped Structure Procheck Summary
LeishBase: Leishmania Structural Database
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