Research workbench
Cryo-EM structure of streptavidin
Analyse Cryo-EM structure of streptavidin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8HRM
- Type
- protein
- Length
- 476 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.56
- Source
- Streptomyces avidinii
- Molecule
- Streptavidin
- UniProt
- P22629
- Pockets
- 2 · best druggability 0.71
Structure
electron microscopy · resolution 2.56 · 1 distinct chain · 3% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Streptavidin | protein | 119 | 3% helix, 55% strand | P22629 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 390 | 0.71 | 0.83 | 69 | empty |
| 2 | 424 | 0.70 | 0.81 | 72 | empty |
Interfaces
6 interfaces between chains.
- B–D · 1525 Ų buried · 21 hydrogen bonds · protein-protein
- A–C · 1507 Ų buried · 22 hydrogen bonds · protein-protein
- A–D · 475 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 473 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 203 Ų buried · 2 hydrogen bonds · protein-protein
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 P22629
- Elsewhere: RCSB PDB 8HRM · PDBe 8HRM · UniProt P22629
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