GL1X · GenesisL1 explorer

MolNFT v1 · #186421 · protein

Crystal structure of TSPAN15 large extracellular loop (TSPAN15 lel)

7RDB · Tetraspanin-15: “Crystal structure of TSPAN15 large extracellular loop (TSPAN15 lel)”. X-ray diffraction, 20 pockets (best druggability 0.80). MolNFT v1 #186421 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
7RDB
Type
protein
Length
2,919 residues
Chains
24
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tetraspanin-15
UniProt
O95858
Pockets
20 · best druggability 0.80

Structure

x-ray diffraction · 4 distinct chains · 47% helix, 3% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
B, A, C, E, F, G, H, I, K, L, M, N, P, Q, R, S, XTetraspanin-15protein12248% helix, 3% strandO95858
D, T, WTetraspanin-15protein12150% helix, 3% strandO95858
J, O, UTetraspanin-15protein12145% helix, 3% strandO95858
VTetraspanin-15protein11947% helix, 3% strandO95858

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16240.800.8572empty
25540.780.8462empty
33510.750.8741empty
411460.750.7885empty
53370.720.8441empty

Interfaces

47 interfaces between chains.

  • E–J · 701 Ų buried · 16 hydrogen bonds · protein-protein
  • A–I · 690 Ų buried · 20 hydrogen bonds · protein-protein
  • D–T · 688 Ų buried · 15 hydrogen bonds · protein-protein
  • B–C · 682 Ų buried · 17 hydrogen bonds · protein-protein
  • G–L · 671 Ų buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 96 disulfide (disulfide).

Compared structures

  • 7RDB · Crystal structure of Tspan15 large extracellular loop (Tspan15 LEL) · the same entry in another collection · chain K against K, TM-score 1.00

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