MolNFT v1 · #157507 · protein
Dihedral oligomeric complex of gyra N-terminal fragment, solved by cryoem in D2 symmetry
6N1Q · DNA gyrase subunit a: “Dihedral oligomeric complex of gyra N-terminal fragment, solved by cryoem in D2 symmetry”. Electron microscopy, 20 pockets (best druggability 0.86). MolNFT v1 #157507 on GenesisL1: 3D structure, binding sites…
- PDB
- 6N1Q
- Type
- protein
- Length
- 3,828 residues
- Chains
- 8
- 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 0.86
Structure
electron microscopy · 2 distinct chains · 47% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G | DNA gyrase subunit a (EC 5.99.1.3) | protein | 476 | 47% helix, 11% strand | A0A0Y2BJX7 |
| B, D, F, H | DNA gyrase subunit a (EC 5.99.1.3) | protein | 481 | 47% helix, 11% 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 | 957 | 0.86 | 0.87 | 151 | empty |
| 2 | 788 | 0.86 | 0.89 | 132 | empty |
| 3 | 816 | 0.85 | 0.87 | 144 | empty |
| 4 | 792 | 0.84 | 0.87 | 129 | empty |
| 5 | 845 | 0.84 | 0.86 | 133 | empty |
Interfaces
14 interfaces between chains.
- A–B · 1078 Ų buried · 17 hydrogen bonds · protein-protein
- G–H · 1078 Ų buried · 17 hydrogen bonds · protein-protein
- C–D · 1073 Ų buried · 17 hydrogen bonds · protein-protein
- E–F · 1073 Ų buried · 17 hydrogen bonds · protein-protein
- A–D · 1067 Ų buried · 50 hydrogen bonds · protein-protein
Compared structures
- 6N1Q · Dihedral oligomeric complex of GyrA N-terminal fragment, solved by cryoEM in D2 symmetry · the same entry in another collection · chain D against D, 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 6N1Q · PDBe 6N1Q · UniProt A0A0Y2BJX7
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