MolNFT v1 · #82588 · protein
Crystal structure of the tyrosine kinase binding domain of cbl-C (pl mutant)
3VRQ · Signal transduction protein cbl-C: “Crystal structure of the tyrosine kinase binding domain of cbl-C (pl mutant)”. X-ray diffraction, 1 ligand (CA), 3 pockets (best druggability 0.68). MolNFT v1 #82588 on GenesisL1: 3D structure…
- PDB
- 3VRQ
- Type
- protein
- Length
- 553 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Signal transduction protein cbl-C
- UniProt
- Q9ULV8
- Ligands
- CA
- Pockets
- 3 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 56% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Signal transduction protein cbl-C | protein | 278 | 56% helix, 10% strand | Q9ULV8 |
| B | Signal transduction protein cbl-C | protein | 275 | 56% helix, 10% strand | Q9ULV8 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 639 | 0.68 | 0.77 | 55 | empty |
| 2 | 604 | 0.66 | 0.76 | 75 | empty |
| 3 | 211 | 0.62 | 0.82 | 33 | empty |
Interfaces
1 interface between chains.
- A–B · 669 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 3VRQ · Crystal structure of the tyrosine kinase binding domain of Cbl-c (PL mutant) · the same entry in another collection · chain A against A, TM-score 1.00
- Q9ULV8 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase cbl-C (Q9ULV8) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q9ULV8
- Elsewhere: RCSB PDB 3VRQ · PDBe 3VRQ · UniProt Q9ULV8
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