Research workbench
Complex of fimc, fimf, fimg and fimh
Analyse Complex of fimc, fimf, fimg and fimh in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3JWN
- Type
- protein
- Length
- 1,859 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein fimc; Protein fimf; Protein fimg; Fimh protein
- UniProt
- P31697, P08189, P08190, Q0T8Y8
- Pockets
- 15 · best druggability 0.65
Structure
x-ray diffraction · 5 distinct chains · 2% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Chaperone protein fimc | protein | 199 | 3% helix, 55% strand | P31697 |
| E, F, K, L | Protein fimf | protein | 154 | 3% helix, 45% strand | P08189 |
| G, M | Protein fimg | protein | 144 | 0% helix, 53% strand | P08190 |
| H, N | Fimh protein | protein | 279 | 2% helix, 52% strand | Q0T8Y8 |
| I | Chaperone protein fimc | protein | 198 | 3% helix, 56% strand | P31697 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains H, N
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 437 | 0.65 | 0.78 | 60 | empty |
| 2 | 330 | 0.61 | 0.78 | 49 | empty |
| 3 | 176 | 0.57 | 0.81 | 37 | empty |
| 4 | 133 | 0.56 | 0.83 | 26 | empty |
| 5 | 125 | 0.43 | 0.77 | 23 | GOL |
Interfaces
11 interfaces between chains.
- I–K · 1678 Ų buried · 34 hydrogen bonds · protein-protein
- C–E · 1657 Ų buried · 34 hydrogen bonds · protein-protein
- G–H · 1331 Ų buried · 31 hydrogen bonds · protein-protein
- M–N · 1323 Ų buried · 28 hydrogen bonds · protein-protein
- L–M · 1300 Ų buried · 35 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
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 P31697
- Every structure of UniProt P08189
- Every structure of UniProt P08190
- Every structure of UniProt Q0T8Y8
- Elsewhere: RCSB PDB 3JWN · PDBe 3JWN · UniProt P31697 · UniProt P08189 · UniProt P08190 · UniProt Q0T8Y8
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