Research workbench
Filaments from ignicoccus hospitalis show diversity of packing in proteins containing N-terminal type IV pilin helices
Analyse Filaments from ignicoccus hospitalis show diversity of packing in proteins… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3J1R
- Type
- protein
- Length
- 546 residues
- Chains
- 21
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Archaeal adhesion filament core
- UniProt
- A8AAA0
- Pockets
- 9 · best druggability 0.68
Structure
electron microscopy · 1 distinct chain · 88% 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 | Archaeal adhesion filament core | protein | 26 | 88% helix, 0% strand | A8AAA0 |
Pockets
9 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 130 | 0.68 | 0.89 | 26 | empty |
| 2 | 126 | 0.67 | 0.88 | 28 | empty |
| 3 | 71 | 0.61 | 0.89 | 18 | empty |
| 4 | 67 | 0.59 | 0.88 | 18 | empty |
| 5 | 62 | 0.58 | 0.88 | 13 | empty |
Interfaces
69 interfaces between chains.
- R–U · 173 Ų buried · 0 hydrogen bonds · protein-protein
- C–F · 173 Ų buried · 0 hydrogen bonds · protein-protein
- F–I · 173 Ų buried · 0 hydrogen bonds · protein-protein
- I–L · 173 Ų buried · 0 hydrogen bonds · protein-protein
- L–O · 173 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3J1R · Filaments from Ignicoccus hospitalis Show Diversity of Packing in Proteins Containing… · 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 A8AAA0
- Elsewhere: RCSB PDB 3J1R · PDBe 3J1R · UniProt A8AAA0
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