Research workbench
Coiled-coil domain-dependent homodimerization of intracellular mla immune receptors defines a minimal functional module for triggering cell death
Analyse Coiled-coil domain-dependent homodimerization of intracellular mla immune… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QFL
- Type
- protein
- Length
- 110 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MLA10
- UniProt
- Q6WWJ4
Structure
x-ray diffraction · 1 distinct chain · 85% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MLA10 | protein | 110 | 85% helix, 0% strand | Q6WWJ4 |
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 3QFL · Coiled-Coil Domain-Dependent Homodimerization of Intracellular MLA Immune Receptors… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q6WWJ4
- Elsewhere: RCSB PDB 3QFL · PDBe 3QFL · UniProt Q6WWJ4
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