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Crystal structure of TSPAN15 large extracellular loop (TSPAN15 lel) in complex with 1C12 Fab

Analyse Crystal structure of TSPAN15 large extracellular loop (TSPAN15 lel) in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7RD5
Type
protein
Length
1,136 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
1C12 Fab light chain; 1C12 Fab heavy chain; Tetraspanin-15
UniProt
O95858
Pockets
11 · best druggability 0.67

Structure

x-ray diffraction · 3 distinct chains · 17% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C1C12 Fab light chainprotein2208% helix, 48% strand—
B, D1C12 Fab heavy chainprotein2268% helix, 47% strand—
F, ETetraspanin-15protein12248% helix, 3% strandO95858

Pockets

11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14480.670.7945empty
23650.640.7947empty
35570.610.7454empty
44520.570.7351empty
51660.460.7630empty

Interfaces

6 interfaces between chains.

  • A–B · 2013 Ų buried · 10 hydrogen bonds · protein-protein
  • C–D · 1993 Ų buried · 10 hydrogen bonds · protein-protein
  • B–F · 551 Ų buried · 3 hydrogen bonds · protein-protein
  • D–E · 543 Ų buried · 4 hydrogen bonds · protein-protein
  • C–E · 220 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 disulfide (disulfide).

Compared structures

  • 7RD5 · Crystal structure of Tspan15 large extracellular loop (Tspan15 LEL) in complex with 1C12… · the same entry in another collection · chain F against F, TM-score 1.00
  • O95858 · AlphaFold monomer V2.0 prediction for tetraspanin-15 (O95858) · a predicted model of the same protein · chain F against A, TM-score 0.91

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