Research workbench
Bacterial gyrb ATPase domain in complex with a chemical fragment
Analyse Bacterial gyrb ATPase domain in complex with a chemical fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Z9M
- Type
- protein
- Length
- 375 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA gyrase subunit B
- EC
- 5.99.1.3
- UniProt
- P0AES6
- Ligands
- BZ2, SO4
- Pockets
- 2 · best druggability 0.48
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA gyrase subunit B (EC 5.99.1.3) | protein | 187 | 29% helix, 30% strand | P0AES6 |
| B | DNA gyrase subunit B (EC 5.99.1.3) | protein | 188 | 30% helix, 30% strand | P0AES6 |
Ligands and binding sites
- BZ2 · 1-benzofuran-2-carboxylic acid · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 11 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 63 | 0.48 | 0.84 | 17 | empty |
| 2 | 50 | 0.33 | 0.78 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 680 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
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 P0AES6
- Elsewhere: RCSB PDB 5Z9M · PDBe 5Z9M · UniProt P0AES6
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