Research workbench
Cryoem structure of PILT4 from geobacter metallireducens without adding nucleotide: C2OOCOOC conformation
Analyse Cryoem structure of PILT4 from geobacter metallireducens without adding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OLL
- Type
- protein
- Length
- 2,114 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Twitching motility pilus retraction ATPase
- UniProt
- Q39VU6
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 2 distinct chains · 40% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D, F | Twitching motility pilus retraction ATPase | protein | 353 | 40% helix, 26% strand | Q39VU6 |
| B, E | Twitching motility pilus retraction ATPase | protein | 351 | 40% helix, 26% strand | Q39VU6 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 942 | 0.83 | 0.85 | 124 | empty |
| 2 | 872 | 0.83 | 0.85 | 115 | empty |
| 3 | 833 | 0.82 | 0.85 | 117 | empty |
| 4 | 1040 | 0.80 | 0.82 | 138 | empty |
| 5 | 696 | 0.80 | 0.85 | 121 | empty |
Interfaces
6 interfaces between chains.
- B–C · 559 Ų buried · 3 hydrogen bonds · protein-protein
- E–F · 556 Ų buried · 3 hydrogen bonds · protein-protein
- D–E · 484 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 482 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 451 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6OLL · CryoEM structure of PilT4 from Geobacter metallireducens without adding nucleotide… · 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 Q39VU6
- Elsewhere: RCSB PDB 6OLL · PDBe 6OLL · UniProt Q39VU6
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