MolNFT v1 · #98813 · protein
Structure of the C-terminal domain of the E. COLI mechanosensitive channel of large conductance
4LKU · Large-conductance mechanosensitive channel: “Structure of the C-terminal domain of the E. COLI mechanosensitive channel of large conductance”. X-ray diffraction, 2 pockets (best druggability 0.72). MolNFT v1 #98813 on GenesisL1: 3D…
- PDB
- 4LKU
- Type
- protein
- Length
- 130 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Large-conductance mechanosensitive channel
- UniProt
- C9QXJ2
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 4 distinct chains · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Large-conductance mechanosensitive channel | protein | 29 | 62% helix, 0% strand | C9QXJ2 |
| C | Large-conductance mechanosensitive channel | protein | 24 | 79% helix, 0% strand | C9QXJ2 |
| D | Large-conductance mechanosensitive channel | protein | 25 | 76% helix, 0% strand | C9QXJ2 |
| E | Large-conductance mechanosensitive channel | protein | 23 | 83% helix, 0% strand | C9QXJ2 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 57 | 0.72 | 0.98 | 23 | empty |
| 2 | 150 | 0.44 | 0.76 | 24 | empty |
Interfaces
9 interfaces between chains.
- A–E · 587 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 567 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 560 Ų buried · 6 hydrogen bonds · protein-protein
- D–E · 549 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 543 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 4LKU · Structure of the C-terminal domain of the E. coli mechanosensitive channel of large… · 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 C9QXJ2
- Elsewhere: RCSB PDB 4LKU · PDBe 4LKU · UniProt C9QXJ2
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