Research workbench
Tetrahedral oligomeric complex of gyra N-terminal fragment, solved by cryoem in tetrahedral symmetry
Analyse Tetrahedral oligomeric complex of gyra N-terminal fragment, solved by cryoem in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6N1R
- Type
- protein
- Length
- 5,796 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA gyrase subunit a
- EC
- 5.99.1.3
- UniProt
- A0A0Y2BJX7
- Pockets
- 20 · best druggability 0.68
Structure
electron microscopy · 1 distinct chain · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | DNA gyrase subunit a (EC 5.99.1.3) | protein | 483 | 48% helix, 14% strand | A0A0Y2BJX7 |
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 | 451 | 0.68 | 0.79 | 73 | empty |
| 2 | 321 | 0.66 | 0.81 | 61 | empty |
| 3 | 467 | 0.63 | 0.77 | 77 | empty |
| 4 | 304 | 0.63 | 0.80 | 59 | empty |
| 5 | 494 | 0.63 | 0.76 | 68 | empty |
Interfaces
30 interfaces between chains.
- A–B · 1197 Ų buried · 19 hydrogen bonds · protein-protein
- D–J · 1196 Ų buried · 19 hydrogen bonds · protein-protein
- H–L · 1195 Ų buried · 19 hydrogen bonds · protein-protein
- E–F · 1195 Ų buried · 19 hydrogen bonds · protein-protein
- C–I · 1193 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 6N1R · Tetrahedral oligomeric complex of GyrA N-terminal fragment, solved by cryoEM in… · the same entry in another collection · chain F against F, 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 A0A0Y2BJX7
- Elsewhere: RCSB PDB 6N1R · PDBe 6N1R · UniProt A0A0Y2BJX7
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