Research workbench
Cryo-EM structure of NLRC4-CARD filament
Analyse Cryo-EM structure of NLRC4-CARD filament in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MKS
- Type
- protein
- Length
- 2,790 residues
- Chains
- 31
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.4
- Source
- Homo sapiens; Vaccinia virus
- Molecule
- Chimera protein of NLR family CARD domain-containing protein 4 and EGFP
- UniProt
- Q9NPP4, A0A1V0D974
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · resolution 3.4 · 1 distinct chain · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b, c, d, e | Chimera protein of NLR family CARD domain-containing protein 4 and EGFP | protein | 90 | 78% helix, 0% strand | Q9NPP4, A0A1V0D974 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 981 | 0.83 | 0.84 | 71 | empty |
| 2 | 932 | 0.82 | 0.84 | 75 | empty |
| 3 | 937 | 0.82 | 0.84 | 72 | empty |
| 4 | 911 | 0.82 | 0.84 | 71 | empty |
| 5 | 900 | 0.82 | 0.84 | 69 | empty |
Interfaces
85 interfaces between chains.
- X–d · 583 Ų buried · 9 hydrogen bonds · protein-protein
- J–P · 582 Ų buried · 9 hydrogen bonds · protein-protein
- C–I · 582 Ų buried · 9 hydrogen bonds · protein-protein
- T–Z · 581 Ų buried · 8 hydrogen bonds · protein-protein
- P–V · 581 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 6MKS · Cryo-EM structure of NLRC4-card filament · 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 Q9NPP4
- Every structure of UniProt A0A1V0D974
- Elsewhere: RCSB PDB 6MKS · PDBe 6MKS · UniProt Q9NPP4 · UniProt A0A1V0D974
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