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Crystal structure of the complex between OX40L and OX40

Analyse Crystal structure of the complex between OX40L and OX40 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2HEV
Type
protein
Length
266 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tumor necrosis factor ligand superfamily member 4; Tumor necrosis factor receptor…
UniProt
P23510, P43489
Ligands
NAG
Pockets
1 · best druggability 0.52

Structure

x-ray diffraction · 2 distinct chains · 1% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
FTumor necrosis factor ligand superfamily member 4protein1260% helix, 61% strandP23510
RTumor necrosis factor receptor superfamily member 4protein1402% helix, 36% strandP43489

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains F, R

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12840.520.7548empty

Interfaces

1 interface between chains.

  • F–R · 490 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

  • 2HEV · Crystal structure of the complex between OX40L and OX40 · the same entry in another collection · chain F against F, TM-score 1.00
  • P23510 · AlphaFold monomer V2.0 prediction for tumor necrosis factor ligand superfamily member 4… · a predicted model of the same protein · chain F against A, TM-score 0.98
  • P43489 · AlphaFold monomer V2.0 prediction for tumor necrosis factor receptor superfamily member 4… · a predicted model of the same protein · chain R against A, TM-score 0.88

Analyse

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