Research workbench
E. COLI DNA gyrase B 24 kda ATPase domain in complex with [3-(3-ethyl- ureido)-5-(pyridin-4-yl)-isoquinolin-8-yl-methyl]-carbamic acid prop- 2-ynyl ester
Analyse E. COLI DNA gyrase B 24 kda ATPase domain in complex with [3-(3-ethyl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MMO
- Type
- protein
- Length
- 206 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA gyrase subunit B
- EC
- 5.99.1.3
- UniProt
- P0AES7
- Ligands
- 9JG, PO4
- Pockets
- 3 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA gyrase subunit B (EC 5.99.1.3) | protein | 206 | 33% helix, 27% strand | P0AES7 |
Ligands and binding sites
- 9JG · prop-2-ynyl ~{N}-[[3-(ethylcarbamoylamino)-5-pyridin-4-yl-isoquinolin-8-yl]methyl]carbamate · ligand · chains A
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 104 | 0.52 | 0.83 | 21 | 9JG |
| 2 | 109 | 0.43 | 0.78 | 20 | empty |
| 3 | 53 | 0.31 | 0.76 | 14 | empty |
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 P0AES7
- Elsewhere: RCSB PDB 5MMO · PDBe 5MMO · UniProt P0AES7
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