Home Research COVID-19 Services Publications People Teaching Job Opening News Forum Lab Only
Online Services

I-TASSER I-TASSER-MTD C-I-TASSER CR-I-TASSER QUARK C-QUARK LOMETS MUSTER CEthreader SEGMER DeepFold DeepFoldRNA FoldDesign COFACTOR COACH MetaGO TripletGO IonCom FG-MD ModRefiner REMO DEMO DEMO-EM SPRING COTH Threpp PEPPI BSpred ANGLOR EDock BSP-SLIM SAXSTER FUpred ThreaDom ThreaDomEx EvoDesign BindProf BindProfX SSIPe GPCR-I-TASSER MAGELLAN ResQ STRUM DAMpred

TM-score TM-align US-align MM-align RNA-align NW-align LS-align EDTSurf MVP MVP-Fit SPICKER HAAD PSSpred 3DRobot MR-REX I-TASSER-MR SVMSEQ NeBcon ResPRE TripletRes DeepPotential WDL-RF ATPbind DockRMSD DeepMSA FASPR EM-Refiner GPU-I-TASSER

BioLiP E. coli GLASS GPCR-HGmod GPCR-RD GPCR-EXP Tara-3D TM-fold DECOYS POTENTIAL RW/RWplus EvoEF HPSF THE-DB ADDRESS Alpaca-Antibody CASP7 CASP8 CASP9 CASP10 CASP11 CASP12 CASP13 CASP14

This page contains 3D structural models (Version 3, built on Aug 2014) of 1,026 putative G protein-coupled receptors (GPCRs) in the human genome generated by the GPCR-I-TASSER pipeline. The most recent (Version 4, built on June 2018) is now available as part of the GPCR-EXP database.

In GPCR-I-TASSER, the GPCR sequences are first threaded through the GPCR template library to identify muliple structure templates by the LOMETS programs. When close homolgous templates are identified, full-length models will be constructed by the I-TASSER based fragment assembly simulations, assisted by a GPCR and membrane specific force field and spatial restraints collected from mutagenesis experiments in GPCR-RD. In case that homologous templates are not available, an ab initio folding procedure is used to assemble the 7-TM-helix bundle from scratch, followed by the GPCR-I-TASSER fragment reassembly simulations. For multiple domain GPCRs, structural models are built by GPCR-I-TASSER for each domain separately which are then reassembly by the I-TASSER approach. All the models are finally subjected to FG-MD for fragment-guided molecular dynamic simulation refinements.

Note:

  • For each entry, the GPCR-HGmod data include top-five full-length models, LOMETS template and alignments, secondary structure prediction, solvent accessibility prediction, and residue-specific error and B-factor predictions.
  • The GPCR-I-TASSER models have generally higher resolution in the transmembrane regions; users should bear cautions on using the loop and tail regions of the models which have usually a relatively lower resolution. Users are encouraged to check the attached residue-specific quality (ResQ) prediction to assess the local structure errors.
  • All the models were constructed from the GPCR sequence alone. An attachment of addition ligand molecules may change the conformation of the structures.
  • Experimentally solved GPCR structures can be found at GPCR-EXP Database.
Other GPCR-related resources
GPCR resources from other laboratories



[ GPCR-HGmod Version 1: Human GPCR structure models generated in Jun 2013 ]
[ GPCR-HGmod Version 2: Human GPCR structure models generated in Mar 2014 ]
[ GPCR-HGmod Version 3: Human GPCR structure models generated in Aug 2014 ]
[ GPCR-HGmod Version 4: Human GPCR structure models generated in Jun 2018 ]

Download the tarball set of all GPCR results

Search GPCR-HGmod by


Structure Models of GPCRs in the Human Genome
<< < 1 2 3 4 5 6 7 8 9 10 > >>
Go to page

HG ID UniProt ID Length C-score Estimated
TM-score
Estimated
RMSD
Top 5 models
HG0001 Q92847 366 0.29 0.75 ± 0.1 6 ± 3.7
HG0002 B9EIL6 312 -0.23 0.68 ± 0.12 6.8 ± 4
HG0003 Q8WZA6 343 -1.5 0.53 ± 0.15 9.9 ± 4.6
HG0004 P30872 391 -0.53 0.65 ± 0.13 7.9 ± 4.4
HG0005 Q6IFB0 361 -1.45 0.54 ± 0.15 9.9 ± 4.6
HG0006 Q8NGC2 313 -0.2 0.69 ± 0.12 6.7 ± 4
HG0007 Q96R27 311 -0.02 0.71 ± 0.12 6.3 ± 3.9
HG0008 Q17RS1 320 -0.3 0.67 ± 0.12 7 ± 4.1
HG0009 Q9H340 312 0.02 0.72 ± 0.11 6.2 ± 3.8
HG0010 A0N0Q0 378 -0.32 0.67 ± 0.13 7.4 ± 4.2


References:

yangzhanglabumich.edu | (734) 647-1549 | 100 Washtenaw Avenue, Ann Arbor, MI 48109-2218