Research workbench
Fully automated NMR structure determination of the ENTH-VHS domain AT3G16270 from Arabidopsis thaliana
Analyse Fully automated NMR structure determination of the ENTH-VHS domain AT3G16270… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DCP
- Type
- protein
- Length
- 140 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- NOT
- Source
- Arabidopsis thaliana
- Molecule
- hypothetical protein (RAFL09-17-B18)
- UniProt
- Q9C5H4
Structure
solution nmr · resolution NOT · 1 distinct chain · 55% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | hypothetical protein (RAFL09-17-B18) | protein | 140 | 55% helix, 1% strand | Q9C5H4 |
Compared structures
- 2DCP · Fully automated NMR structure determination of the enth-vhs domain AT3G16270 from… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9C5H4 · AlphaFold monomer V2.0 prediction for protein modified transport to the vacuole 1 (Q9C5H4) · a predicted model of the same protein · chain A against A, TM-score 0.87
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 Q9C5H4
- Elsewhere: RCSB PDB 2DCP · PDBe 2DCP · UniProt Q9C5H4
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