Research workbench
Lipid II flippase murj, inward closed conformation
Analyse Lipid II flippase murj, inward closed conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NC6
- Type
- protein
- Length
- 927 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipid II flippase murj
- UniProt
- B7IE18
- Ligands
- OLB, ZN, NA, CL
- Pockets
- 9 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 84% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipid II flippase murj | protein | 466 | 84% helix, 0% strand | B7IE18 |
| B | Lipid II flippase murj | protein | 461 | 84% helix, 0% strand | B7IE18 |
Ligands and binding sites
- OLB · (2S)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · ligand · chains A
- ZN · Zinc ion · metal · 2 copies · chains A, B
- NA · Sodium ion · metal · chains A
- CL · Chloride ion · ion · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 860 | 0.82 | 0.84 | 56 | empty |
| 2 | 751 | 0.82 | 0.85 | 64 | empty |
| 3 | 254 | 0.67 | 0.82 | 28 | empty |
| 4 | 226 | 0.63 | 0.82 | 33 | empty |
| 5 | 188 | 0.45 | 0.73 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 330 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
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 B7IE18
- Elsewhere: RCSB PDB 6NC6 · PDBe 6NC6 · UniProt B7IE18
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