Research workbench
Crystal structure of the receiver domain of the ethylene receptor of arabidopsis thaliana
Analyse Crystal structure of the receiver domain of the ethylene receptor of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DCF
- Type
- protein
- Length
- 133 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ETR1 protein
- EC
- 2.7.3.-
- UniProt
- P49333
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ETR1 protein (EC 2.7.3.-) | protein | 133 | 38% helix, 19% strand | P49333 |
Compared structures
- 1DCF · Crystal structure of the receiver domain of the ethylene receptor of arabidopsis thaliana · the same entry in another collection · chain A against A, TM-score 1.00
- P49333 · AlphaFold monomer V2.0 prediction for ethylene receptor 1 (P49333) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P49333
- Elsewhere: RCSB PDB 1DCF · PDBe 1DCF · UniProt P49333
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