GPCR CLASS (FAMILY)
GPCR SPECIES
GPCR PREFERRED CHAIN
G PROTEIN (FAMILY)
G PROTEIN SPECIES
PDB CODE
RESOLUTION
REFERENCE
PUBLICATION DATE
LIGAND INTERACTIONS
LIGANDS
Apo (no ligand) - Apo (no ligand)
PHYSIOLOGICAL LIGANDS
No physiological ligands available
GPCR - G protein interface interactions
The biflare plot is a modified version of a flareplot, where lines are drawn between an inner concentric circle
(Gα residues)
and an outer concentric circle (GPCR residues) depicting the interface interactions.
Different interaction types are shown with different line types (aromatic - solid,
hydrophobic - dashed,
ionic - long dashed, polar - dotted, Van der Waals - dash-dot).
The interactive features include filtering on interaction type, segments, residues and backbone or sidechain interactions.
GPCR-G protein backbone (bb) or sidechain (sc):
Structures
0 structures selected.
Sequence Color
Interaction frequency filter (%)
Gα,
Gβ,
Gγ,
GPCR
Interaction cut-off: strict (stick), loose (line)
Interaction type |
GPCR Segment |
AA |
Number |
Generic number |
Gα segment |
AA |
Number |
Generic number |
---|---|---|---|---|---|---|---|---|
Hydrophobic | TM6 | L | 1150 | 6x45 | G.H5 | L | 393 | G.H5.25 |
Hydrophobic | ICL2 | F | 1041 | - | G.S3 | V | 217 | G.S3.01 |
Hydrophobic | ICL2 | F | 1041 | - | G.H5 | K | 380 | G.H5.12 |
Hydrophobic | ICL2 | V | 1040 | - | G.H5 | L | 384 | G.H5.16 |
Hydrophobic | ICL2 | V | 1040 | - | G.H5 | I | 383 | G.H5.15 |
Van-der-waals | ICL2 | V | 1040 | - | G.H5 | I | 383 | G.H5.15 |
Hydrophobic | ICL2 | F | 1041 | - | G.S1 | L | 41 | G.S1.02 |
Hydrophobic | ICL2 | F | 1041 | - | G.H5 | F | 376 | G.H5.08 |
Van-der-waals | ICL2 | F | 1041 | - | G.H5 | F | 376 | G.H5.08 |
Hydrophobic | ICL3 | T | 1118 | - | G.H5 | V | 394 | G.H5.26 |
Van-der-waals | ICL3 | T | 1118 | - | G.H5 | V | 394 | G.H5.26 |
Polar | TM3 | M | 1036 | 3x57 | G.H5 | N | 387 | G.H5.19 |
Van-der-waals | TM3 | M | 1036 | 3x57 | G.H5 | N | 387 | G.H5.19 |
Ionic | ICL2 | E | 1042 | - | G.hns1 | R | 38 | G.hns1.02 |
Polar | ICL2 | E | 1042 | - | G.hns1 | R | 38 | G.hns1.02 |
Van-der-waals | ICL2 | E | 1042 | - | G.hns1 | R | 38 | G.hns1.02 |
Ionic | TM5 | H | 1117 | 5x64 | G.H5 | D | 381 | G.H5.13 |
Hydrophobic | ICL2 | V | 1040 | - | G.H5 | K | 380 | G.H5.12 |
Hydrophobic | TM5 | H | 1117 | 5x64 | G.H5 | L | 384 | G.H5.16 |
Hydrophobic | TM3 | L | 1037 | 3x58 | G.H5 | N | 387 | G.H5.19 |
Hydrophobic | TM3 | L | 1037 | 3x58 | G.H5 | L | 388 | G.H5.20 |
Van-der-waals | TM3 | L | 1037 | 3x58 | G.H5 | L | 388 | G.H5.20 |
Polar | TM2 | R | 977 | 2x46 | G.H5 | Y | 391 | G.H5.23 |
Aromatic | TM2 | R | 977 | 2x46 | G.H5 | Y | 391 | G.H5.23 |
Hydrophobic | TM2 | R | 977 | 2x46 | G.H5 | Y | 391 | G.H5.23 |
Polar | H8 | Q | 1195 | 8x47 | G.H5 | N | 392 | G.H5.24 |
Polar | TM5 | H | 1117 | 5x64 | G.H5 | Q | 385 | G.H5.17 |
Van-der-waals | TM5 | H | 1117 | 5x64 | G.H5 | Q | 385 | G.H5.17 |
Hydrophobic | TM3 | L | 1033 | 3x54 | G.H5 | Y | 391 | G.H5.23 |
Hydrophobic | TM5 | M | 1114 | 5x61 | G.H5 | L | 393 | G.H5.25 |
Van-der-waals | TM5 | M | 1114 | 5x61 | G.H5 | L | 393 | G.H5.25 |
Polar | ICL2 | E | 1044 | - | G.HN | Q | 35 | G.HN.52 |
Ionic | H8 | K | 1197 | 8x49 | G.H5 | E | 390 | G.H5.22 |
Polar | H8 | K | 1197 | 8x49 | G.H5 | E | 390 | G.H5.22 |
Van-der-waals | H8 | K | 1197 | 8x49 | G.H5 | E | 390 | G.H5.22 |
Hydrophobic | TM3 | L | 1037 | 3x58 | G.H5 | L | 384 | G.H5.16 |
Hydrophobic | ICL2 | E | 1042 | - | G.hns1 | R | 39 | G.hns1.03 |
Hydrophobic | ICL2 | F | 1041 | - | G.H5 | I | 383 | G.H5.15 |
Van-der-waals | ICL2 | F | 1041 | - | G.H5 | I | 383 | G.H5.15 |
Hydrophobic | TM3 | M | 1036 | 3x57 | G.H5 | Y | 391 | G.H5.23 |
Van-der-waals | TM3 | M | 1036 | 3x57 | G.H5 | Y | 391 | G.H5.23 |
Hydrophobic | TM5 | M | 1114 | 5x61 | G.H5 | V | 394 | G.H5.26 |
Van-der-waals | TM5 | M | 1114 | 5x61 | G.H5 | V | 394 | G.H5.26 |