Research workbench
Protein fibril
Analyse Protein fibril in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KIB
- Type
- protein
- Length
- 56 residues
- Chains
- 8
- Method
- solid-state nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nfgail segment from human islet amyloid polypeptide
- Pockets
- 2 · best druggability 0.67
Structure
solid-state nmr · 1 distinct chain · 0% helix, 71% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Nfgail segment from human islet amyloid polypeptide | protein | 7 | 0% helix, 71% strand | — |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 109 | 0.67 | 0.90 | 29 | empty |
| 2 | 65 | 0.35 | 0.77 | 21 | empty |
Interfaces
14 interfaces between chains.
- A–E · 310 Ų buried · 12 hydrogen bonds · protein-protein
- B–F · 293 Ų buried · 12 hydrogen bonds · protein-protein
- F–H · 277 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 275 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 259 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 2KIB · Protein Fibril · 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
- Elsewhere: RCSB PDB 2KIB · PDBe 2KIB
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