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Crystal structure of a 20KDA fragment of flgg
Analyse Crystal structure of a 20KDA fragment of flgg in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6JF2
- Type
- protein
- Length
- 301 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellar basal-body rod protein flgg
- UniProt
- P0A1J3
- Pockets
- 3 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 2% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flagellar basal-body rod protein flgg | protein | 145 | 2% helix, 45% strand | P0A1J3 |
| B | Flagellar basal-body rod protein flgg | protein | 156 | 2% helix, 41% strand | P0A1J3 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 107 | 0.40 | 0.76 | 24 | empty |
| 2 | 83 | 0.33 | 0.74 | 17 | empty |
| 3 | 64 | 0.30 | 0.74 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 249 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
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 P0A1J3
- Elsewhere: RCSB PDB 6JF2 · PDBe 6JF2 · UniProt P0A1J3
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