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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
HG0020 Q9Y5X5 522 -2.2 0.45 ± 0.15 9.99 ± 4.2
HG0021 Q6IFR1 324 -0.72 0.62 ± 0.14 7.9 ± 4.4
HG0022 Q8NGK1 321 -0.42 0.66 ± 0.13 7.3 ± 4.2
HG0023 Q8NGJ0 315 -0.11 0.7 ± 0.12 6.5 ± 3.9
HG0024 P47884 311 0 0.71 ± 0.11 6.3 ± 3.8
HG0025 Q96RI9 348 -0.2 0.69 ± 0.12 6.9 ± 4.1
HG0026 P29371 465 -2.5 0.42 ± 0.14 9.99 ± 4.1
HG0027 P08173 479 -0.4 0.66 ± 0.13 8.1 ± 4.4
HG0028 Q5CZ62 431 -1.65 0.51 ± 0.15 9.99 ± 4.6
HG0029 P21462 350 0.02 0.72 ± 0.11 6.5 ± 3.9
HG0030 P0C628 307 -0.13 0.7 ± 0.12 6.5 ± 3.9


References:

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