Research workbench
Cryoem structure of the type IV pilin PILA5 from thermus thermophilus
Analyse Cryoem structure of the type IV pilin PILA5 from thermus thermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XXE
- Type
- protein
- Length
- 1,776 residues
- Chains
- 16
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- Q72GL2
- Pockets
- 16 · best druggability 0.74
Structure
electron microscopy · 1 distinct chain · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P | Uncharacterized protein | protein | 111 | 41% helix, 17% strand | Q72GL2 |
Pockets
16 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 862 | 0.74 | 0.78 | 63 | empty |
| 2 | 237 | 0.51 | 0.75 | 32 | empty |
| 3 | 231 | 0.49 | 0.75 | 32 | empty |
| 4 | 197 | 0.47 | 0.75 | 28 | empty |
| 5 | 125 | 0.42 | 0.76 | 21 | empty |
Interfaces
84 interfaces between chains.
- L–O · 992 Ų buried · 11 hydrogen bonds · protein-protein
- B–E · 992 Ų buried · 11 hydrogen bonds · protein-protein
- D–G · 992 Ų buried · 11 hydrogen bonds · protein-protein
- I–L · 992 Ų buried · 11 hydrogen bonds · protein-protein
- M–P · 990 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 disulfide (disulfide).
Compared structures
- 6XXE · CryoEM structure of the type IV pilin PilA5 from Thermus thermophilus · the same entry in another collection · chain P against P, 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 Q72GL2
- Elsewhere: RCSB PDB 6XXE · PDBe 6XXE · UniProt Q72GL2
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