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Crystal structure of trichoplax adhaerens trbcl-2L2 bound to trbak BH3

Analyse Crystal structure of trichoplax adhaerens trbcl-2L2 bound to trbak BH3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6YLD
Type
protein
Length
347 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
BCL-2-like protein 1; BCL-2 homologous ANTAGONIST/KILLER
UniProt
A0A369S2N9, A0A369S334
Pockets
1 · best druggability 0.50

Structure

x-ray diffraction · 4 distinct chains · 78% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABCL-2-like protein 1protein15077% helix, 0% strandA0A369S2N9
BBCL-2 homologous ANTAGONIST/KILLERprotein2488% helix, 0% strandA0A369S334
CBCL-2-like protein 1protein15276% helix, 0% strandA0A369S2N9
DBCL-2 homologous ANTAGONIST/KILLERprotein2181% helix, 0% strandA0A369S334

Ligands and binding sites

  • EDO · 1,2-ethanediol · additive · 3 copies · chains A, C
  • TAR · D(-)-tartaric acid · additive · 3 copies · chains A, C

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
11630.500.7826empty

Interfaces

5 interfaces between chains.

  • C–D · 1013 Ų buried · 12 hydrogen bonds · protein-protein
  • A–B · 984 Ų buried · 10 hydrogen bonds · protein-protein
  • B–C · 359 Ų buried · 2 hydrogen bonds · protein-protein
  • A–C · 339 Ų buried · 7 hydrogen bonds · protein-protein
  • B–D · 12 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 6YLD · Crystal structure of Trichoplax adhaerens trBcl-2L2 bound to trBak BH3 · the same entry in another collection · chain A against A, TM-score 1.00

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