Research workbench
Molecular structure of the interleukin-1 receptor- associated kinase-4 death domain
Analyse Molecular structure of the interleukin-1 receptor- associated kinase-4 death… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2A9I
- Type
- protein
- Length
- 105 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interleukin-1 receptor-associated kinase-4
- EC
- 2.7.1.37
- UniProt
- Q8R4K2
- Ligands
- MN
Structure
x-ray diffraction · 1 distinct chain · 63% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interleukin-1 receptor-associated kinase-4 (EC 2.7.1.37) | protein | 105 | 63% helix, 4% strand | Q8R4K2 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2A9I · Molecular Structure of the Interleukin-1 Receptor-Associated Kinase-4 Death Domain · the same entry in another collection · chain A against A, TM-score 1.00
- Q8R4K2 · AlphaFold monomer V2.0 prediction for interleukin-1 receptor- associated kinase 4 (Q8R4K2) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q8R4K2
- Elsewhere: RCSB PDB 2A9I · PDBe 2A9I · UniProt Q8R4K2
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.