Research workbench
The structural versatility of tasa in B. subtilis biofilm formation
Analyse The structural versatility of tasa in B. subtilis biofilm formation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OF2
- Type
- protein
- Length
- 191 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P54507
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 191 | — | P54507 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5OF2 · The structural versatility of TasA in B. subtilis biofilm formation · the same entry in another collection · chain A against A, TM-score 1.00
- P54507 · AlphaFold monomer V2.0 prediction for major biofilm matrix component (P54507) · a predicted model of the same protein · chain A against A, TM-score 0.83
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 P54507
- Elsewhere: RCSB PDB 5OF2 · PDBe 5OF2 · UniProt P54507
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