Research workbench
Cryo-EM structure of the plectasin fibril (double strands)
Analyse Cryo-EM structure of the plectasin fibril (double strands) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OAE
- Type
- protein
- Length
- 1,680 residues
- Chains
- 42
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fungal defensin plectasin
- UniProt
- Q53I06
- Pockets
- 20 · best druggability 0.80
Structure
electron microscopy · 1 distinct chain · 38% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, C, D, E, F, G, H, I, J, K, L, M, N, T, U, A, O, P, Q, R, S, V, W, X, Y, Z, 0, 1, 2, 3, 4, 5, 6, 7, 8, 9, a, b, c, d, e, f | Fungal defensin plectasin | protein | 40 | 38% helix, 20% strand | Q53I06 |
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 | 620 | 0.80 | 0.85 | 103 | empty |
| 2 | 487 | 0.78 | 0.86 | 91 | empty |
| 3 | 573 | 0.78 | 0.84 | 103 | empty |
| 4 | 454 | 0.75 | 0.84 | 83 | empty |
| 5 | 153 | 0.73 | 0.92 | 36 | empty |
Interfaces
155 interfaces between chains.
- C–F · 465 Ų buried · 3 hydrogen bonds · protein-protein
- A–Q · 464 Ų buried · 3 hydrogen bonds · protein-protein
- 3–6 · 461 Ų buried · 2 hydrogen bonds · protein-protein
- W–Z · 460 Ų buried · 2 hydrogen bonds · protein-protein
- J–M · 460 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 126 disulfide (disulfide).
Compared structures
- 7OAE · Cryo-EM structure of the plectasin fibril (double strands) · the same entry in another collection · chain L against L, 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 Q53I06
- Elsewhere: RCSB PDB 7OAE · PDBe 7OAE · UniProt Q53I06
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