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Crystal structure of the human glucagon receptor (gcgr) in complex with the antagonist mk-0893

Analyse Crystal structure of the human glucagon receptor (gcgr) in complex with the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5EE7
Type
protein
Length
416 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glucagon RECEPTOR,ENDOLYSIN,GLUCAGON receptor
EC
3.2.1.17
UniProt
P47871, P00720
Ligands
OLA, 5MV
Pockets
5 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 76% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlucagon RECEPTOR,ENDOLYSIN,GLUCAGON receptor (EC 3.2.1.17)protein41676% helix, 4% strandP47871, P00720

Ligands and binding sites

  • OLA · Oleic acid · ligand · 14 copies · chains A
  • 5MV · 3-[[4-[(1~{S})-1-[3-[3,5-bis(chloranyl)phenyl]-5-(6-methoxynaphthalen-2-yl)pyrazol-1-yl]ethyl]phenyl]carbonylamino]propanoic acid · ligand · chains A
  • PE5 · 3,6,9,12,15,18,21,24-octaoxahexacosan-1-ol · additive · chains A
  • TLA · L(+)-tartaric acid · additive · chains A

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12000.770.9129PE5
24290.620.7644empty
3970.440.7925empty
4540.380.8013empty
51100.370.7421empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 5EE7 · Crystal structure of the human glucagon receptor (GCGR) in complex with the antagonist… · the same entry in another collection · chain A against A, TM-score 1.00
  • P47871 · AlphaFold monomer V2.0 prediction for glucagon receptor (P47871) · a predicted model of the same protein · chain A against A, TM-score 0.55

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