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MolNFT v1 · #38451 · protein

2.7 a structure of the extracellular domains of the human beta common receptor involved in il-3, il-5, and gm-csf signalling

2GYS · Cytokine receptor common beta chain: “2.7 a structure of the extracellular domains of the human beta common receptor involved in il-3, il-5, and…”. X-ray diffraction, 3 ligands (NAG, FUC, BMA), 8 pockets (best druggability 0.49).…

PDB
2GYS
Type
protein
Length
803 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cytokine receptor common beta chain
Ligands
NAG, FUC, BMA
Pockets
8 · best druggability 0.49

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 47% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACytokine receptor common beta chainprotein3976% helix, 47% strand—
BCytokine receptor common beta chainprotein4066% helix, 47% strand—

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B
  • FUC · alpha-L-fucopyranose · sugar · 4 copies · chains A, B
  • BMA · beta-D-mannopyranose · sugar · 2 copies

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

Pockets

8 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1990.490.8117empty
22560.480.7337empty
31370.460.7725empty
41910.430.7321empty
51360.390.7319empty

Interfaces

1 interface between chains.

  • A–B · 4941 Ų buried · 84 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide, 4 glycan (disulfide, N-glycosylation).

Compared structures

  • 2GYS · 2.7 A structure of the extracellular domains of the human beta common receptor involved… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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