Research workbench
Crystal structure of the propionibacterium acnes surface sialidase
Analyse Crystal structure of the propionibacterium acnes surface sialidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LBU
- Type
- protein
- Length
- 380 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Exo-alpha-sialidase
- UniProt
- A0A2B7IY20
- Ligands
- PO4
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Exo-alpha-sialidase | protein | 380 | 3% helix, 43% strand | A0A2B7IY20 |
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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 163 | 0.82 | 0.97 | 24 | empty |
| 2 | 114 | 0.47 | 0.79 | 20 | ACT |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 7LBU · Crystal structure of the Propionibacterium acnes surface sialidase · 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 A0A2B7IY20
- Elsewhere: RCSB PDB 7LBU · PDBe 7LBU · UniProt A0A2B7IY20
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