Research workbench
NMR structure of the hypothetical enth-vhs domain AT3G16270 from arabidopsis thaliana
Analyse NMR structure of the hypothetical enth-vhs domain AT3G16270 from arabidopsis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VDY
- Type
- protein
- Length
- 140 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein (RAFL09-17-B18)
- UniProt
- Q9C5H4
Structure
solution nmr · 1 distinct chain · 58% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein (RAFL09-17-B18) | protein | 140 | 58% helix, 0% strand | Q9C5H4 |
Compared structures
- 1VDY · NMR Structure of the hypothetical ENTH-VHS domain At3g16270 from Arabidopsis thaliana · 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 1VDY · PDBe 1VDY · UniProt Q9C5H4
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