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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

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Structure Models of GPCRs in the Human Genome
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HG ID UniProt ID Length C-score Estimated
TM-score
Estimated
RMSD
Top 5 models
HG0190 P46095 362 0.07 0.72 ± 0.11 6.4 ± 3.9
HG0191 Q8NGZ9 312 -0.3 0.68 ± 0.12 6.9 ± 4.1
HG0192 Q9H343 314 -0.23 0.68 ± 0.12 6.8 ± 4
HG0193 Q8NH93 324 -0.31 0.67 ± 0.12 7 ± 4.1
HG0194 Q7Z3T1 314 -0.05 0.71 ± 0.12 6.4 ± 3.9
HG0195 Q9H208 303 0.57 0.79 ± 0.09 5 ± 3.3
HG0196 Q8N7J6 304 -0.65 0.63 ± 0.13 7.6 ± 4.3
HG0197 P25089 353 -0.37 0.67 ± 0.13 7.4 ± 4.2
HG0198 Q8TDU6 330 -0.02 0.71 ± 0.12 6.4 ± 3.9
HG0199 P43657 344 -0.66 0.63 ± 0.14 8 ± 4.4
HG0200 A1A4V4 400 -0.49 0.65 ± 0.13 7.9 ± 4.4


References:

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