Research workbench
Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains, quadruple mutant, I222 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
- 4QES
- Type
- protein
- Length
- 1,323 residues
- Chains
- 3
- 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
- 14 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Non-haem bromoperoxidase bpo-A2, matrix protein 1 chimera (EC 1.11.1.-) | protein | 441 | 54% helix, 12% strand | P29715, P03485 |
Pockets
14 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1180 | 0.84 | 0.85 | 107 | empty |
| 2 | 307 | 0.59 | 0.77 | 39 | empty |
| 3 | 244 | 0.56 | 0.78 | 35 | empty |
| 4 | 266 | 0.56 | 0.77 | 36 | empty |
| 5 | 123 | 0.55 | 0.82 | 22 | empty |
Interfaces
3 interfaces between chains.
- A–C · 944 Ų buried · 21 hydrogen bonds · protein-protein
- B–C · 918 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 913 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 4QES · Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains… · the same entry in another collection · chain A against A, TM-score 1.00
- P29715 · AlphaFold monomer V2.0 prediction for non-haem bromoperoxidase bpo-A2 (P29715) · a predicted model of the same protein · chain A against A, TM-score 0.63
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 4QES · PDBe 4QES · UniProt P29715 · UniProt P03485
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