Research workbench
Lptbfgc from enterobacter cloacae
Analyse Lptbfgc from enterobacter cloacae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MIT
- Type
- protein
- Length
- 2,657 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipopolysaccharide export system ATP-binding protein; Lipopolysaccharide export system…
- UniProt
- A0A0H3CR83, A0A0H3CU18, A0A232G4N0, A0A0H3CQA2
- Ligands
- NOV, SO4, CL
- Pockets
- 20 · best druggability 0.74
Structure
x-ray diffraction · 7 distinct chains · 52% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D | Lipopolysaccharide export system ATP-binding protein | protein | 240 | 37% helix, 22% strand | A0A0H3CR83 |
| C, H | Lipopolysaccharide export system protein lptc | protein | 175 | 12% helix, 54% strand | A0A0H3CU18 |
| F | Lps export ABC transporter permease lptf | protein | 350 | 59% helix, 15% strand | A0A232G4N0 |
| G | Lipopolysaccharide export system permease protein lptg | protein | 355 | 63% helix, 15% strand | A0A0H3CQA2 |
| E | Lipopolysaccharide export system ATP-binding protein | protein | 238 | 40% helix, 26% strand | A0A0H3CR83 |
| I | Lps export ABC transporter permease lptf | protein | 335 | 60% helix, 13% strand | A0A232G4N0 |
| J | Lipopolysaccharide export system permease protein lptg | protein | 309 | 70% helix, 7% strand | A0A0H3CQA2 |
Ligands and binding sites
- NOV · Novobiocin · ligand · chains B, E
- SO4 · Sulfate ion · ion · 11 copies · chains A, B, F, G, D, E, I, J
- CL · Chloride ion · ion · chains A
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 | 517 | 0.74 | 0.82 | 55 | empty |
| 2 | 438 | 0.74 | 0.83 | 47 | empty |
| 3 | 830 | 0.73 | 0.78 | 83 | empty |
| 4 | 1120 | 0.73 | 0.76 | 106 | SO4 |
| 5 | 679 | 0.73 | 0.79 | 79 | empty |
Interfaces
15 interfaces between chains.
- C–F · 1298 Ų buried · 15 hydrogen bonds · protein-protein
- F–G · 1281 Ų buried · 5 hydrogen bonds · protein-protein
- H–I · 1227 Ų buried · 14 hydrogen bonds · protein-protein
- B–F · 1065 Ų buried · 10 hydrogen bonds · protein-protein
- E–I · 1049 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 6MIT · LptBFGC from Enterobacter cloacae · the same entry in another collection · chain I against I, 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 A0A0H3CR83
- Every structure of UniProt A0A0H3CU18
- Every structure of UniProt A0A232G4N0
- Every structure of UniProt A0A0H3CQA2
- Elsewhere: RCSB PDB 6MIT · PDBe 6MIT · UniProt A0A0H3CR83 · UniProt A0A0H3CU18 · UniProt A0A232G4N0 · UniProt A0A0H3CQA2
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