Research workbench
Refined structure of the actin-severing domain villin 14T, determined by solution NMR, minimized average structure
Analyse Refined structure of the actin-severing domain villin 14T, determined by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VIK
- Type
- protein
- Length
- 126 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Villin 14T
- UniProt
- P02640
Structure
solution nmr · 1 distinct chain · 21% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Villin 14T | protein | 126 | 21% helix, 24% strand | P02640 |
Compared structures
- 2VIK · Refined structure of the actin-severing domain villin 14T, determined by solution NMR… · the same entry in another collection · chain A against A, TM-score 1.00
- P02640 · AlphaFold monomer V2.0 prediction for villin-1 (P02640) · a predicted model of the same protein · chain A against A, TM-score 0.80
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 P02640
- Elsewhere: RCSB PDB 2VIK · PDBe 2VIK · UniProt P02640
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