Research workbench
Cryo-EM structure of NLRP1-DPP9-vbp complex
Analyse Cryo-EM structure of NLRP1-DPP9-vbp complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6X6C
- Type
- protein
- Length
- 1,964 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q86TI2, Q9C000
- Ligands
- GK2
Structure
electron microscopy · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | — | protein | 846 | — | Q86TI2 |
| E | — | protein | 134 | — | Q9C000 |
| F | — | protein | 138 | — | Q9C000 |
Ligands and binding sites
- GK2 · [(2~{R})-1-[(2~{R})-2-azanyl-3-methyl-butanoyl]pyrrolidin-2-yl]boronic acid · ligand · 2 copies · chains A, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6X6C · Cryo-EM structure of NLRP1-DPP9-VbP complex · the same entry in another collection · chain F against F, TM-score 1.00
- Q86TI2 · AlphaFold monomer V2.0 prediction for dipeptidyl peptidase 9 (Q86TI2) · a predicted model of the same protein · chain A against A, TM-score 0.99
- Q9C000 · AlphaFold monomer V2.0 prediction for nacht, lrr and pyd domains- containing protein 1… · a predicted model of the same protein · chain F against A, TM-score 0.90
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 Q86TI2
- Every structure of UniProt Q9C000
- Elsewhere: RCSB PDB 6X6C · PDBe 6X6C · UniProt Q86TI2 · UniProt Q9C000
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