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Heterotrimeric complex of PHOSDUCIN/TRANSDUCIN beta-gamma

Analyse Heterotrimeric complex of PHOSDUCIN/TRANSDUCIN beta-gamma in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1A0R
Type
protein
Length
592 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transducin (beta subunit); Transducin (gamma subunit); Phosducin
UniProt
P04901, P02698, P19632
Ligands
ACE, FAR
Pockets
6 · best druggability 0.79

Structure

x-ray diffraction · 3 distinct chains · 25% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BTransducin (beta subunit)protein3399% helix, 46% strandP04901
GTransducin (gamma subunit)protein6560% helix, 0% strandP02698
PPhosducinprotein18843% helix, 15% strandP19632

Ligands and binding sites

  • ACE · Acetyl group · ligand · chains B, G
  • FAR · Farnesyl · ligand · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15790.790.8551empty
24900.700.8061FAR
33410.630.7939empty
4970.560.8516empty
51170.470.7929empty

Interfaces

3 interfaces between chains.

  • B–G · 2602 Ų buried · 23 hydrogen bonds · protein-protein
  • B–P · 2223 Ų buried · 42 hydrogen bonds · protein-protein
  • G–P · 28 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 1A0R · Heterotrimeric complex of PHOSDUCIN/TRANSDUCIN beta-gamma · the same entry in another collection · chain B against B, TM-score 1.00
  • P19632 · AlphaFold monomer V2.0 prediction for phosducin (P19632) · a predicted model of the same protein · chain P against A, TM-score 0.97
  • P02698 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(T) subunit… · a predicted model of the same protein · chain G against A, TM-score 0.94

Analyse

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