FPR2/ALX - Gi2

GPCR CLASS (FAMILY)

Class A (Rhodopsin)

GPCR SPECIES

Homo sapiens

GPCR PREFERRED CHAIN

R

G PROTEIN (FAMILY)

Gi/o

G PROTEIN SPECIES

Homo sapiens

PDB CODE

RESOLUTION

3.0 Å

REFERENCE

PUBLICATION DATE

April 13, 2022

3D VIEW

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LIGAND INTERACTIONS

LIGANDS

Amyloid beta-Peptide (1-42) - Agonist pubchem

PHYSIOLOGICAL LIGANDS

LXA4, serum amyloid A, PrP106-126, aspirin-triggered resolvin D1, humanin, aspirin triggered lipoxin A4, LL-37, annexin I, resolvin D1



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.


Interaction cut-off:

Residue numbering:

GPCR-G protein backbone (bb) or sidechain (sc):





Structures

Sequence Color

, , , GPCR
Interaction cut-off: strict (stick), loose (line)

NGL is a WebGL based 3D viewer powered by MMTF.

Interaction
type
GPCR
Segment

AA

Number
Generic
number

segment

AA

Number
Generic
number
Hydrophobic ICL2 P 130 34x50 G.H5 I 344 G.H5.15
Van-der-waals ICL2 P 130 34x50 G.H5 I 344 G.H5.15
Polar TM6 R 238 6x32 G.H5 L 354 G.H5.25
Hydrophobic TM5 I 228 5x65 G.H5 I 345 G.H5.16
Polar TM6 P 239 6x33 G.H5 L 354 G.H5.25
Hydrophobic TM6 P 239 6x33 G.H5 L 354 G.H5.25
Van-der-waals TM6 P 239 6x33 G.H5 L 354 G.H5.25
Hydrophobic ICL2 Q 134 34x54 G.S3 L 195 G.S3.01
Polar TM4 S 140 4x40 G.HN E 28 G.HN.52
Polar ICL2 N 135 34x55 G.s2s3 D 194 G.s2s3.02
Van-der-waals ICL2 N 135 34x55 G.s2s3 D 194 G.s2s3.02
Hydrophobic ICL3 M 233 - G.H5 K 346 G.H5.17
Van-der-waals ICL3 M 233 - G.H5 K 346 G.H5.17
Aromatic ICL2 H 136 34x56 G.hns1 R 32 G.hns1.03
Polar TM6 R 238 6x32 G.H5 G 353 G.H5.24
Polar TM3 C 126 3x53 G.H5 N 348 G.H5.19
Hydrophobic TM3 C 126 3x53 G.H5 N 348 G.H5.19
Hydrophobic ICL2 V 131 34x51 G.H5 F 337 G.H5.08
Van-der-waals ICL2 V 131 34x51 G.H5 F 337 G.H5.08
Polar ICL2 N 135 34x55 G.hns1 R 32 G.hns1.03
Hydrophobic ICL2 N 135 34x55 G.hns1 R 32 G.hns1.03
Van-der-waals ICL2 N 135 34x55 G.hns1 R 32 G.hns1.03
Polar ICL2 Q 134 34x54 G.hns1 A 31 G.hns1.02
Hydrophobic TM5 K 227 5x64 G.H5 I 345 G.H5.16
Hydrophobic ICL2 P 130 34x50 G.H5 I 345 G.H5.16
Van-der-waals ICL2 P 130 34x50 G.H5 I 345 G.H5.16
Hydrophobic ICL3 M 233 - G.H5 I 345 G.H5.16
Van-der-waals ICL3 M 233 - G.H5 I 345 G.H5.16
Hydrophobic ICL3 M 233 - G.H5 F 355 G.H5.26
Hydrophobic TM5 I 228 5x65 G.H5 L 349 G.H5.20
Hydrophobic ICL2 V 131 34x51 G.S3 L 195 G.S3.01
Hydrophobic TM5 I 224 5x61 G.H5 L 354 G.H5.25
Hydrophobic ICL2 Q 134 34x54 G.S1 V 34 G.S1.02
Van-der-waals ICL2 Q 134 34x54 G.S1 V 34 G.S1.02
Ionic ICL3 K 235 - G.h4s6 E 319 G.h4s6.12
Polar ICL3 K 235 - G.h4s6 E 319 G.h4s6.12
Hydrophobic TM2 T 60 2x39 G.H5 C 352 G.H5.23
Polar TM2 Y 64 2x43 G.H5 C 352 G.H5.23
Van-der-waals TM2 Y 64 2x43 G.H5 C 352 G.H5.23
Hydrophobic TM6 L 243 6x37 G.H5 L 354 G.H5.25
Van-der-waals TM6 L 243 6x37 G.H5 L 354 G.H5.25
Hydrophobic TM7 V 305 7x56 G.H5 G 353 G.H5.24
Hydrophobic ICL2 P 130 34x50 G.H5 T 341 G.H5.12
Van-der-waals ICL2 P 130 34x50 G.H5 T 341 G.H5.12
Hydrophobic ICL2 Q 134 34x54 G.H5 I 344 G.H5.15
Hydrophobic TM4 T 138 4x38 G.HN E 28 G.HN.52
Van-der-waals TM4 T 138 4x38 G.HN E 28 G.HN.52
Polar TM6 R 238 6x32 G.H5 F 355 G.H5.26
Hydrophobic H8 G 306 8x47 G.H5 G 353 G.H5.24
Hydrophobic TM3 V 127 3x54 G.H5 L 349 G.H5.20
Van-der-waals TM3 V 127 3x54 G.H5 L 349 G.H5.20
Hydrophobic TM6 P 239 6x33 G.H5 F 355 G.H5.26
Van-der-waals TM6 P 239 6x33 G.H5 F 355 G.H5.26
Hydrophobic ICL2 V 131 34x51 G.s2s3 D 194 G.s2s3.02
Van-der-waals ICL2 V 131 34x51 G.s2s3 D 194 G.s2s3.02
Polar TM3 R 123 3x50 G.H5 C 352 G.H5.23
Hydrophobic TM3 R 123 3x50 G.H5 C 352 G.H5.23
Van-der-waals TM3 R 123 3x50 G.H5 C 352 G.H5.23
Hydrophobic ICL2 Q 134 34x54 G.hns1 R 32 G.hns1.03