Research workbench
Crystal structure of the brox BRO1 domain in complex with the C- terminal tail of CHMP4B
Analyse Crystal structure of the brox BRO1 domain in complex with the C- terminal tail… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UM3
- Type
- protein
- Length
- 395 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BRO1 domain-containing protein brox; Charged multivesicular body protein 4B
- UniProt
- Q5VW32, Q9H444
- Pockets
- 3 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 61% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | BRO1 domain-containing protein brox | protein | 377 | 61% helix, 2% strand | Q5VW32 |
| B | Charged multivesicular body protein 4B | protein | 18 | 72% helix, 0% strand | Q9H444 |
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 | 161 | 0.55 | 0.81 | 29 | empty |
| 2 | 56 | 0.39 | 0.80 | 17 | empty |
| 3 | 90 | 0.35 | 0.74 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 750 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 3UM3 · Crystal structure of the Brox Bro1 domain in complex with the C-terminal tail of CHMP4B · the same entry in another collection · chain A against A, TM-score 1.00
- Q5VW32 · AlphaFold monomer V2.0 prediction for BRO1 domain-containing protein brox (Q5VW32) · a predicted model of the same protein · chain A against A, TM-score 0.99
- Q9H444 · AlphaFold monomer V2.0 prediction for charged multivesicular body protein 4B (Q9H444) · a predicted model of the same protein · chain B against A, TM-score 0.50
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 Q5VW32
- Every structure of UniProt Q9H444
- Elsewhere: RCSB PDB 3UM3 · PDBe 3UM3 · UniProt Q5VW32 · UniProt Q9H444
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