Research workbench
Structure of the catalytic domain of ETR1 from arabidopsis thaliana
Analyse Structure of the catalytic domain of ETR1 from arabidopsis thaliana in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PL9
- Type
- protein
- Length
- 150 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ethylene receptor 1
- EC
- 2.7.13.3
- UniProt
- P49333
- Ligands
- ADP, CD, CL
- Pockets
- 1 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ethylene receptor 1 (EC 2.7.13.3) | protein | 150 | 36% helix, 30% strand | P49333 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- CD · Cadmium ion · metal · 11 copies · chains A
- CL · Chloride ion · ion · chains A
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 208 | 0.56 | 0.79 | 31 | CD, CL, ADP |
Compared structures
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 4PL9 · PDBe 4PL9 · UniProt P49333
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