Research workbench
Structure of the N-terminal domain of cbl in complex with its binding site in zap-70
Analyse Structure of the N-terminal domain of cbl in complex with its binding site in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1B47
- Type
- protein
- Length
- 912 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cbl
- UniProt
- P22681
- Ligands
- CA
- Pockets
- 13 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 59% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Cbl | protein | 304 | 59% helix, 9% strand | P22681 |
Ligands and binding sites
- CA · Calcium ion · metal · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 909 | 0.71 | 0.75 | 99 | empty |
| 2 | 607 | 0.65 | 0.75 | 61 | empty |
| 3 | 478 | 0.61 | 0.75 | 57 | empty |
| 4 | 252 | 0.53 | 0.76 | 38 | empty |
| 5 | 123 | 0.50 | 0.80 | 21 | empty |
Interfaces
2 interfaces between chains.
- A–B · 809 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 752 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 1B47 · Structure of the N-terminal domain of cbl in complex with its binding site in zap-70 · the same entry in another collection · chain A against A, TM-score 1.00
- P22681 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase cbl (P22681) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P22681
- Elsewhere: RCSB PDB 1B47 · PDBe 1B47 · UniProt P22681
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