Research workbench
Stractural insight into the interaction between escrt-III and VPS4
Analyse Stractural insight into the interaction between escrt-III and VPS4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2V6X
- Type
- protein
- Length
- 123 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vacuolar protein sorting-associated protein 4; DOA4-independent degradation protein 4
- EC
- 3.6.4.6
- UniProt
- P52917, P36108
- Ligands
- SO4
Structure
x-ray diffraction · 2 distinct chains · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar protein sorting-associated protein 4 (EC 3.6.4.6) | protein | 82 | 83% helix, 0% strand | P52917 |
| B | DOA4-independent degradation protein 4 | protein | 41 | 46% helix, 0% strand | P36108 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1353 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 2V6X · Stractural insight into the interaction between ESCRT-III and Vps4 · the same entry in another collection · chain A against A, TM-score 1.00
- P52917 · AlphaFold monomer V2.0 prediction for vacuolar protein sorting- associated protein 4… · a predicted model of the same protein · chain A against A, TM-score 0.91
- P36108 · AlphaFold monomer V2.0 prediction for DOA4-independent degradation protein 4 (P36108) · a predicted model of the same protein · chain B against A, TM-score 0.33
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 P52917
- Every structure of UniProt P36108
- Elsewhere: RCSB PDB 2V6X · PDBe 2V6X · UniProt P52917 · UniProt P36108
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