Research workbench
Structure of the F-bar domain of mouse syndapin I
Analyse Structure of the F-bar domain of mouse syndapin I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2X3V
- Type
- protein
- Length
- 874 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q61644
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 291 | — | Q61644 |
| B | — | protein | 292 | — | Q61644 |
Compared structures
- 2X3V · Structure of The F-BAR Domain of Mouse Syndapin I · the same entry in another collection · chain A against A, TM-score 1.00
- Q61644 · AlphaFold monomer V2.0 prediction for protein kinase C and casein kinase substrate in… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q61644
- Elsewhere: RCSB PDB 2X3V · PDBe 2X3V · UniProt Q61644
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