Research workbench
Crystal structure of arabidopsis NRG1.1 cc-R domain K94E/K96E mutant
Analyse Crystal structure of arabidopsis NRG1.1 cc-R domain K94E/K96E mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7L7W
- Type
- protein
- Length
- 118 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable disease resistance protein AT5G66900
- UniProt
- Q9FKZ1
- Ligands
- NI
Structure
x-ray diffraction · 1 distinct chain · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable disease resistance protein AT5G66900 | protein | 118 | 75% helix, 0% strand | Q9FKZ1 |
Ligands and binding sites
- NI · Nickel (II) ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7L7W · Crystal structure of Arabidopsis NRG1.1 CC-R domain K94E/K96E mutant · the same entry in another collection · chain A against A, TM-score 1.00
- Q9FKZ1 · AlphaFold monomer V2.0 prediction for probable disease resistance protein AT5G66900… · a predicted model of the same protein · chain A against A, TM-score 0.83
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 Q9FKZ1
- Elsewhere: RCSB PDB 7L7W · PDBe 7L7W · UniProt Q9FKZ1
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