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Crystal structure of CASPASE8 tded
Analyse Crystal structure of CASPASE8 tded in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JQE
- Type
- protein
- Length
- 544 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sugar ABC transporter substrate-binding PROTEIN,CASPASE-8 chimera
- EC
- 3.4.22.61
- UniProt
- A0A0L7A8Z3, Q14790
- Pockets
- 3 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sugar ABC transporter substrate-binding PROTEIN,CASPASE-8 chimera (EC 3.4.22.61) | protein | 544 | 50% helix, 14% strand | A0A0L7A8Z3, Q14790 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 601 | 0.68 | 0.77 | 86 | empty |
| 2 | 93 | 0.38 | 0.76 | 15 | empty |
| 3 | 60 | 0.29 | 0.74 | 15 | empty |
Compared structures
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 A0A0L7A8Z3
- Every structure of UniProt Q14790
- Elsewhere: RCSB PDB 5JQE · PDBe 5JQE · UniProt A0A0L7A8Z3 · UniProt Q14790
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