Research workbench
2.1A X-ray structure of tolc: an integral outer membrane protein and efflux pump component from escherichia COLI
Analyse 2.1A X-ray structure of tolc: an integral outer membrane protein and efflux… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EK9
- Type
- protein
- Length
- 1,284 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Outer membrane protein tolc
- UniProt
- P02930
- Pockets
- 15 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 67% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Outer membrane protein tolc | protein | 428 | 67% helix, 16% strand | P02930 |
Pockets
15 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 898 | 0.72 | 0.77 | 107 | empty |
| 2 | 181 | 0.46 | 0.75 | 24 | empty |
| 3 | 178 | 0.45 | 0.74 | 25 | empty |
| 4 | 163 | 0.45 | 0.75 | 24 | empty |
| 5 | 98 | 0.40 | 0.76 | 22 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2581 Ų buried · 60 hydrogen bonds · protein-protein
- B–C · 2576 Ų buried · 65 hydrogen bonds · protein-protein
- A–C · 2562 Ų buried · 60 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 15 modified (engineered).
Compared structures
- 1EK9 · 2.1A X-ray structure of tolc: an integral outer membrane protein and efflux pump… · the same entry in another collection · chain A against A, TM-score 1.00
- P02930 · AlphaFold monomer V2.0 prediction for outer membrane protein tolc (P02930) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P02930
- Elsewhere: RCSB PDB 1EK9 · PDBe 1EK9 · UniProt P02930
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