Research workbench
NMR structure of the hypothetical rhodanese domain AT4G01050 from arabidopsis thaliana
Analyse NMR structure of the hypothetical rhodanese domain AT4G01050 from arabidopsis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VEE
- Type
- protein
- Length
- 134 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proline-rich protein family
- UniProt
- Q9M158
Structure
solution nmr · 1 distinct chain · 34% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proline-rich protein family | protein | 134 | 34% helix, 16% strand | Q9M158 |
Compared structures
- 1VEE · NMR structure of the hypothetical rhodanese domain At4g01050 from Arabidopsis thaliana · the same entry in another collection · chain A against A, TM-score 1.00
- Q9M158 · AlphaFold monomer V2.0 prediction for rhodanese-like domain- containing protein 4… · a predicted model of the same protein · chain A against A, TM-score 0.90
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 Q9M158
- Elsewhere: RCSB PDB 1VEE · PDBe 1VEE · UniProt Q9M158
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