Research workbench
Cryo-EM structure of the ATP-bound VPS4 mutant-E233Q hexamer (masked)
Analyse Cryo-EM structure of the ATP-bound VPS4 mutant-E233Q hexamer (masked) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XMI
- Type
- protein
- Length
- 1,914 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P52917
- Ligands
- ATP
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | — | protein | 319 | — | P52917 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 5 copies · chains B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5XMI · Cryo-EM Structure of the ATP-bound VPS4 mutant-E233Q hexamer (masked) · the same entry in another collection · chain C against C, 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 0.88
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
- Elsewhere: RCSB PDB 5XMI · PDBe 5XMI · UniProt P52917
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