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Crystal structure of stall-1 and bcma

Analyse Crystal structure of stall-1 and bcma in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1OQD
Type
protein
Length
1,734 residues
Chains
18
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tumor necrosis factor ligand superfamily member 13B, soluble form; Tumor necrosis factor…
UniProt
Q9Y275, Q02223
Pockets
20 · best druggability 0.75

Structure

x-ray diffraction · 3 distinct chains · 8% helix, 47% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, JTumor necrosis factor ligand superfamily member 13B, soluble formprotein1440% helix, 56% strandQ9Y275
K, L, M, O, P, Q, RTumor necrosis factor receptor superfamily member 17protein3933% helix, 21% strandQ02223
NTumor necrosis factor receptor superfamily member 17protein2119% helix, 29% strandQ02223

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1580.750.9913empty
21390.750.9320empty
3590.740.9912empty
41270.740.9320empty
5540.740.9912empty

Interfaces

38 interfaces between chains.

  • E–F · 996 Ų buried · 26 hydrogen bonds · protein-protein
  • G–I · 996 Ų buried · 24 hydrogen bonds · protein-protein
  • D–E · 993 Ų buried · 29 hydrogen bonds · protein-protein
  • D–F · 990 Ų buried · 24 hydrogen bonds · protein-protein
  • H–I · 989 Ų buried · 27 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 32 disulfide (disulfide).

Compared structures

  • 1OQD · Crystal structure of sTALL-1 and BCMA · the same entry in another collection · chain R against R, TM-score 1.00

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