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Structure of the bacillus anthracis sap S-layer assembly domain
Analyse Structure of the bacillus anthracis sap S-layer assembly domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HHU
- Type
- protein
- Length
- 830 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- S-layer protein sap; Nanobody AF684; Nanobody AF694
- UniProt
- P49051
- Pockets
- 8 · best druggability 0.62
Structure
x-ray diffraction · 3 distinct chains · 4% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-layer protein sap | protein | 588 | 4% helix, 52% strand | P49051 |
| G | Nanobody AF684 | protein | 119 | 3% helix, 54% strand | — |
| H | Nanobody AF694 | protein | 123 | 5% helix, 51% strand | — |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 61 | 0.62 | 0.92 | 20 | empty |
| 2 | 444 | 0.61 | 0.75 | 52 | empty |
| 3 | 275 | 0.58 | 0.78 | 33 | empty |
| 4 | 75 | 0.45 | 0.82 | 19 | empty |
| 5 | 143 | 0.42 | 0.75 | 26 | empty |
Interfaces
2 interfaces between chains.
- A–G · 1118 Ų buried · 18 hydrogen bonds · protein-protein
- A–H · 625 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified, 2 disulfide (engineered, disulfide).
Compared structures
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 P49051
- Elsewhere: RCSB PDB 6HHU · PDBe 6HHU · UniProt P49051
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