Research workbench
Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains, quadruple mutant, P212121 form
Analyse Structure of a 16 nm protein cage designed by fusing symmetric oligomeric… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QFF
- Type
- protein
- Length
- 5,292 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Non-haem bromoperoxidase bpo-A2, matrix protein 1 chimera
- EC
- 1.11.1.-
- UniProt
- P29715, P03485
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | Non-haem bromoperoxidase bpo-A2, matrix protein 1 chimera (EC 1.11.1.-) | protein | 441 | 54% helix, 12% strand | P29715, P03485 |
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 | 1020 | 0.87 | 0.88 | 147 | empty |
| 2 | 1026 | 0.86 | 0.87 | 146 | empty |
| 3 | 1058 | 0.86 | 0.87 | 123 | empty |
| 4 | 1173 | 0.84 | 0.85 | 120 | empty |
| 5 | 738 | 0.66 | 0.74 | 73 | empty |
Interfaces
22 interfaces between chains.
- A–H · 1145 Ų buried · 19 hydrogen bonds · protein-protein
- F–L · 1129 Ų buried · 11 hydrogen bonds · protein-protein
- C–E · 1113 Ų buried · 11 hydrogen bonds · protein-protein
- G–K · 1108 Ų buried · 9 hydrogen bonds · protein-protein
- D–I · 1097 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 4QFF · Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains… · 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 P29715
- Every structure of UniProt P03485
- Elsewhere: RCSB PDB 4QFF · PDBe 4QFF · UniProt P29715 · UniProt P03485
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