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Crystal structure of human tetraspanin CD81

Analyse Crystal structure of human tetraspanin CD81 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5TCX
Type
protein
Length
208 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
CD81 antigen
UniProt
P60033
Ligands
CLR
Pockets
2 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 81% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACD81 antigenprotein20881% helix, 0% strandP60033

Ligands and binding sites

  • CLR · Cholesterol · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11420.510.7919CLR
22310.490.7432empty

Modifications

Observed in the structure: 2 disulfide, 2 modified (disulfide, alkylation).

Compared structures

  • P60033 · AlphaFold monomer V2.0 prediction for CD81 antigen (P60033) · a predicted model of the same protein · chain A against A, TM-score 0.98

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