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View Structure Prediction Details

Protein: HMGCR
Organism: Homo sapiens
Length: 888 amino acids
Reference: Drew K, et al. (2011) The proteome folding project: Proteome-scale prediction of structure and function. Genome Res. 2011 Sep 16



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Top Sequence Alignment Hits

Listed below are up to the top 10 sequence alignment matches, by species, for the PSI-BLAST search against the protein sequence for HMGCR.

Description E-value Query
Range
Subject
Range
gi|114599629, gi... - gi|114599629|ref|XP_001148405.1| PREDICTED: 3-hydroxy-3-methylglutaryl-Coenzyme A reductase isoform ...
0.0 [1..888] [1..888]
HMDH_PONPY - 3-hydroxy-3-methylglutaryl-coenzyme A reductase - Pongo pygmaeus (Orangutan)
HMDH_PONAB - 3-hydroxy-3-methylglutaryl-coenzyme A reductase OS=Pongo abelii GN=HMGCR PE=2 SV=1
0.0 [1..888] [1..888]
gi|109077611 - gi|109077611|ref|XP_001104607.1| PREDICTED: 3-hydroxy-3-methylglutaryl-Coenzyme A reductase isoform ...
0.0 [1..888] [1..888]
gi|76626437 - gi|76626437|ref|XP_605365.2| PREDICTED: similar to 3-hydroxy-3-methylglutaryl-coenzyme A reductase (...
0.0 [1..888] [91..978]
HMDH_RABIT - 3-hydroxy-3-methylglutaryl-coenzyme A reductase OS=Oryctolagus cuniculus GN=HMGCR PE=3 SV=1
0.0 [1..888] [1..888]
gi|73952215 - gi|73952215|ref|XP_536323.2| PREDICTED: similar to 3-hydroxy-3-methylglutaryl-coenzyme A reductase (...
0.0 [1..888] [1..888]
HMDH_MOUSE - 3-hydroxy-3-methylglutaryl-coenzyme A reductase OS=Mus musculus GN=Hmgcr PE=2 SV=2
0.0 [1..888] [1..887]
HMDH_PIG - 3-hydroxy-3-methylglutaryl-coenzyme A reductase OS=Sus scrofa GN=HMGCR PE=2 SV=1
0.0 [1..888] [1..885]
HMDH_MESAU - 3-hydroxy-3-methylglutaryl-coenzyme A reductase OS=Mesocricetus auratus GN=HMGCR PE=1 SV=1
0.0 [1..888] [1..887]

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Predicted Domain #1
Region A:
Residues: [1-513]
      1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 MLSRLFRMHG LFVASHPWEV IVGTVTLTIC MMSMNMFTGN NKICGWNYEC PKFEEDVLSS  60
   61 DIIILTITRC IAILYIYFQF QNLRQLGSKY ILGIAGLFTI FSSFVFSTVV IHFLDKELTG 120
  121 LNEALPFFLL LIDLSRASTL AKFALSSNSQ DEVRENIARG MAILGPTFTL DALVECLVIG 180
  181 VGTMSGVRQL EIMCCFGCMS VLANYFVFMT FFPACVSLVL ELSRESREGR PIWQLSHFAR 240
  241 VLEEEENKPN PVTQRVKMIM SLGLVLVHAH SRWIADPSPQ NSTADTSKVS LGLDENVSKR 300
  301 IEPSVSLWQF YLSKMISMDI EQVITLSLAL LLAVKYIFFE QTETESTLSL KNPITSPVVT 360
  361 QKKVPDNCCR REPMLVRNNQ KCDSVEEETG INRERKVEVI KPLVAETDTP NRATFVVGNS 420
  421 SLLDTSSVLV TQEPEIELPR EPRPNEECLQ ILGNAEKGAK FLSDAEIIQL VNAKHIPAYK 480
  481 LETLMETHER GVSIRRQLLS KKLSEPSSLQ YLP

[Run NCBI BLAST on this sequence.]

Detection Method: PSI-BLAST
Confidence: 71.522879
Match: 1oy6A
Description: Multidrug efflux transporter AcrB pore domain; PN1, PN2, PC1 and PC2 subdomains; Multidrug efflux transporter AcrB TolC docking domain; DN and DC subdomains; Multidrug efflux transporter AcrB transmembrane domain
Matching Structure (courtesy of the PDB):

Predicted Domain #2
Region A:
Residues: [514-888]
      1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 YRDYNYSLVM GACCENVIGY MPIPVGVAGP LCLDEKEFQV PMATTEGCLV ASTNRGCRAI  60
   61 GLGGGASSRV LADGMTRGPV VRLPRACDSA EVKAWLETSE GFAVIKEAFD STSRFARLQK 120
  121 LHTSIAGRNL YIRFQSRSGD AMGMNMISKG TEKALSKLHE YFPEMQILAV SGNYCTDKKP 180
  181 AAINWIEGRG KSVVCEAVIP AKVVREVLKT TTEAMIEVNI NKNLVGSAMA GSIGGYNAHA 240
  241 ANIVTAIYIA CGQDAAQNVG SSNCITLMEA SGPTNEDLYI SCTMPSIEIG TVGGGTNLLP 300
  301 QQACLQMLGV QGACKDNPGE NARQLARIVC GTVMAGELSL MAALAAGHLV KSHMIHNRSK 360
  361 INLQDLQGAC TKKTA

[Run NCBI BLAST on this sequence.]

Detection Method: PSI-BLAST
Confidence: 1000.0
Match: 1dq8A
Description: NAD-binding domain of HMG-CoA reductase; Substrate-binding domain of HMG-CoA reductase
Matching Structure (courtesy of the PDB):

YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle