Research workbench
The crystal structure of ospa mutant
Analyse The crystal structure of ospa mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2I5Z
- Type
- protein
- Length
- 246 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Outer surface protein a
- UniProt
- Q45040
- Pockets
- 2 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| O | Outer surface protein a | protein | 246 | 4% helix, 55% strand | Q45040 |
Ligands and binding sites
- PG4 · Tetraethylene glycol · additive · chains O
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 | 113 | 0.46 | 0.79 | 25 | empty |
| 2 | 104 | 0.38 | 0.75 | 20 | PG4 |
Compared structures
- 2I5Z · The crystal structure of OspA mutant · the same entry in another collection · chain O against O, 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 Q45040
- Elsewhere: RCSB PDB 2I5Z · PDBe 2I5Z · UniProt Q45040
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