Research workbench
Structure of the ERS1 dimerization and histidine phosphotransfer domain from arabidopsis thaliana
Analyse Structure of the ERS1 dimerization and histidine phosphotransfer domain from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MT8
- Type
- protein
- Length
- 196 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ethylene response sensor 1
- EC
- 2.7.11.-, 2.7.13.3
- UniProt
- Q38846
Structure
x-ray diffraction · 2 distinct chains · 89% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ethylene response sensor 1 (EC 2.7.11.-, 2.7.13.3) | protein | 100 | 90% helix, 0% strand | Q38846 |
| B | Ethylene response sensor 1 (EC 2.7.11.-, 2.7.13.3) | protein | 96 | 88% helix, 0% strand | Q38846 |
Interfaces
1 interface between chains.
- A–B · 2085 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 4MT8 · Structure of the ERS1 dimerization and histidine phosphotransfer domain from Arabidopsis… · the same entry in another collection · chain A against A, TM-score 1.00
- Q38846 · AlphaFold monomer V2.0 prediction for ethylene response sensor 1 (Q38846) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 Q38846
- Elsewhere: RCSB PDB 4MT8 · PDBe 4MT8 · UniProt Q38846
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