Research workbench
Structure of gldlm, the proton-powered motor that drives protein transport and gliding motility
Analyse Structure of gldlm, the proton-powered motor that drives protein transport and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6YS8
- Type
- protein
- Length
- 737 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gldm; Gldl
- UniProt
- Q5EGM3, Q5EGM4
- Pockets
- 8 · best druggability 0.82
Structure
electron microscopy · 3 distinct chains · 67% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gldm | protein | 218 | 64% helix, 3% strand | Q5EGM3 |
| B | Gldm | protein | 219 | 70% helix, 2% strand | Q5EGM3 |
| G, F, E, D, C | Gldl | protein | 60 | 65% helix, 0% strand | Q5EGM4 |
Pockets
8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 206 | 0.82 | 0.95 | 41 | empty |
| 2 | 549 | 0.80 | 0.86 | 76 | empty |
| 3 | 462 | 0.71 | 0.81 | 53 | empty |
| 4 | 895 | 0.71 | 0.76 | 77 | empty |
| 5 | 351 | 0.71 | 0.83 | 36 | empty |
Interfaces
15 interfaces between chains.
- A–B · 1843 Ų buried · 14 hydrogen bonds · protein-protein
- A–E · 732 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 571 Ų buried · 1 hydrogen bond · protein-protein
- G–C · 568 Ų buried · 1 hydrogen bond · protein-protein
- G–F · 559 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6YS8 · Structure of GldLM, the proton-powered motor that drives protein transport and gliding… · 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 Q5EGM3
- Every structure of UniProt Q5EGM4
- Elsewhere: RCSB PDB 6YS8 · PDBe 6YS8 · UniProt Q5EGM3 · UniProt Q5EGM4
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