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Crystal structure of the peptidoglycan O-acetyltransferase B (PatB) from Campylobacter jejuni, catalytic domain
Analyse Crystal structure of the peptidoglycan O-acetyltransferase B (PatB) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8TLB
- Type
- protein
- Length
- 214 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.9
- Source
- Campylobacter jejuni
- Molecule
- Peptidoglycan O-acetyltransferase B (PatB)
- EC
- 2.3.1.-
- UniProt
- A0A0H3PJC1
- Ligands
- CL
- Pockets
- 1 · best druggability 0.44
Structure
x-ray diffraction · resolution 1.9 · 1 distinct chain · 36% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidoglycan O-acetyltransferase B (PatB) (EC 2.3.1.-) | protein | 214 | 36% helix, 21% strand | A0A0H3PJC1 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.44 | 0.84 | 17 | empty |
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 A0A0H3PJC1
- Elsewhere: RCSB PDB 8TLB · PDBe 8TLB · UniProt A0A0H3PJC1
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