Research workbench
Single particle reconstruction of hemq from geobacillus based on data acquired in the presence of substantial aberrations
Analyse Single particle reconstruction of hemq from geobacillus based on data acquired… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VSA
- Type
- protein
- Length
- 1,175 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemq
- EC
- 1.11.1.-
- UniProt
- A0A0E0TGF4
- Pockets
- 20 · best druggability 0.67
Structure
electron microscopy · 1 distinct chain · 40% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| V, W, X, Y, Z | Hemq (EC 1.11.1.-) | protein | 235 | 40% helix, 31% strand | A0A0E0TGF4 |
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 587 | 0.67 | 0.76 | 36 | empty |
| 2 | 508 | 0.66 | 0.77 | 37 | empty |
| 3 | 519 | 0.65 | 0.77 | 42 | empty |
| 4 | 558 | 0.65 | 0.76 | 41 | empty |
| 5 | 503 | 0.64 | 0.76 | 39 | empty |
Interfaces
5 interfaces between chains.
- X–Y · 1759 Ų buried · 31 hydrogen bonds · protein-protein
- V–W · 1756 Ų buried · 30 hydrogen bonds · protein-protein
- X–Z · 1754 Ų buried · 30 hydrogen bonds · protein-protein
- W–Y · 1750 Ų buried · 31 hydrogen bonds · protein-protein
- V–Z · 1750 Ų buried · 30 hydrogen bonds · protein-protein
Compared structures
- 6VSA · Single particle reconstruction of HemQ from Geobacillus based on data acquired in the… · the same entry in another collection · chain V against V, 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 A0A0E0TGF4
- Elsewhere: RCSB PDB 6VSA · PDBe 6VSA · UniProt A0A0E0TGF4
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