MolNFT v1 · #159316 · protein
Cryoem structure of PILT4 from geobacter metallireducens with added ATP: C6CCCCCC conformation
6OLM · Twitching motility pilus retraction ATPase: “Cryoem structure of PILT4 from geobacter metallireducens with added ATP: C6CCCCCC conformation”. Electron microscopy, 1 ligand (ATP), 20 pockets (best druggability 0.83). MolNFT v1…
- PDB
- 6OLM
- Type
- protein
- Length
- 2,112 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Twitching motility pilus retraction ATPase
- UniProt
- Q39VU6
- Ligands
- ATP
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 1 distinct chain · 42% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Twitching motility pilus retraction ATPase | protein | 352 | 42% helix, 27% strand | Q39VU6 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 903 | 0.83 | 0.86 | 131 | empty |
| 2 | 888 | 0.83 | 0.85 | 130 | empty |
| 3 | 940 | 0.83 | 0.85 | 138 | empty |
| 4 | 860 | 0.83 | 0.85 | 121 | empty |
| 5 | 1128 | 0.82 | 0.83 | 131 | empty |
Interfaces
6 interfaces between chains.
- A–B · 565 Ų buried · 3 hydrogen bonds · protein-protein
- D–E · 565 Ų buried · 3 hydrogen bonds · protein-protein
- A–F · 565 Ų buried · 3 hydrogen bonds · protein-protein
- E–F · 564 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 563 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 6OLM · CryoEM structure of PilT4 from Geobacter metallireducens with added ATP: C6cccccc… · 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 6OLM · PDBe 6OLM · UniProt Q39VU6
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