Research workbench
Inactive choanoflagellate E3 ubiquitin ligase cbl tkb
Analyse Inactive choanoflagellate E3 ubiquitin ligase cbl tkb in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BK5
- Type
- protein
- Length
- 323 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin ligase cbl
- UniProt
- F2UL73
- Ligands
- CA
- Pockets
- 2 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 56% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ubiquitin ligase cbl | protein | 323 | 56% helix, 9% strand | F2UL73 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 180 | 0.58 | 0.81 | 29 | empty |
| 2 | 127 | 0.53 | 0.81 | 24 | empty |
Compared structures
- 6BK5 · Inactive choanoflagellate E3 ubiquitin ligase Cbl TKB · 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 F2UL73
- Elsewhere: RCSB PDB 6BK5 · PDBe 6BK5 · UniProt F2UL73
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