Research workbench
Tandem yvtn beta-propeller and pkd domains from an archaeal surface layer protein
Analyse Tandem yvtn beta-propeller and pkd domains from an archaeal surface layer… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1L0Q
- Type
- protein
- Length
- 1,564 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Surface layer protein
- UniProt
- Q50245
- Pockets
- 11 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 1% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Surface layer protein | protein | 391 | 1% helix, 57% strand | Q50245 |
Pockets
11 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 546 | 0.75 | 0.83 | 54 | empty |
| 2 | 528 | 0.75 | 0.83 | 58 | empty |
| 3 | 542 | 0.73 | 0.81 | 59 | empty |
| 4 | 363 | 0.66 | 0.80 | 36 | empty |
| 5 | 185 | 0.64 | 0.84 | 30 | empty |
Interfaces
5 interfaces between chains.
- A–C · 317 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 281 Ų buried · 1 hydrogen bond · protein-protein
- C–D · 246 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 185 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 136 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 modified (engineered, alkylation).
Compared structures
- 1L0Q · Tandem YVTN beta-propeller and PKD domains from an archaeal surface layer protein · 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 Q50245
- Elsewhere: RCSB PDB 1L0Q · PDBe 1L0Q · UniProt Q50245
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