Research workbench
Structure of Chlamydia abortus effector protein ChlaDUB
Analyse Structure of Chlamydia abortus effector protein ChlaDUB in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GZU
- Type
- protein
- Length
- 241 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.47
- Source
- Chlamydia abortus
- Molecule
- Conserved membrane protein
- UniProt
- Q5L5G1
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.41
Structure
x-ray diffraction · resolution 1.47 · 1 distinct chain · 38% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Conserved membrane protein | protein | 241 | 38% helix, 13% strand | Q5L5G1 |
Ligands and binding sites
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 | 98 | 0.41 | 0.78 | 19 | empty |
| 2 | 61 | 0.40 | 0.81 | 18 | empty |
Compared structures
- 6GZU · Structure of chlamydia abortus effector protein chladub · the same entry in another collection · chain A against A, 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 Q5L5G1
- Elsewhere: RCSB PDB 6GZU · PDBe 6GZU · UniProt Q5L5G1
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