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The crystal structure of ail, the attachment invasion locus protein of yersinia pestis
Analyse The crystal structure of ail, the attachment invasion locus protein of yersinia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QRA
- Type
- protein
- Length
- 152 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Attachment invasion locus protein
- UniProt
- Q0WCZ9
- Pockets
- 1 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 74% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Attachment invasion locus protein | protein | 152 | 0% helix, 74% strand | Q0WCZ9 |
Ligands and binding sites
- C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 7 copies · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 200 | 0.51 | 0.76 | 28 | C8E |
Compared structures
- 3QRA · The crystal structure of Ail, the attachment invasion locus protein of Yersinia pestis · 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 Q0WCZ9
- Elsewhere: RCSB PDB 3QRA · PDBe 3QRA · UniProt Q0WCZ9
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