MolNFT v2 · #172583 · protein
Crystal structure of Trichoplax adhaerens trBcl-2L2 bound to trBak BH3
6YLD: “Crystal structure of Trichoplax adhaerens trBcl-2L2 bound to trBak BH3”. X-ray diffraction at 1.4. MolNFT v2 #172583 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6YLD
- Type
- protein
- Length
- 347 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.4
- Source
- Trichoplax sp. H2; SYNTHETIC CONSTRUCT
- UniProt
- A0A369S2N9, A0A369S334
Structure
x-ray diffraction · resolution 1.4 · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 150 | — | A0A369S2N9 |
| B | — | protein | 24 | — | A0A369S334 |
| C | — | protein | 152 | — | A0A369S2N9 |
| D | — | protein | 21 | — | A0A369S334 |
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.
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
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A0A369S2N9
- Every structure of UniProt A0A369S334
- Elsewhere: RCSB PDB 6YLD · PDBe 6YLD · UniProt A0A369S2N9 · UniProt A0A369S334
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