Research workbench
Conformational Transition between Four- and Five-stranded Phenylalanine Zippers Determined by a Local Packing Interaction
Analyse Conformational Transition between Four- and Five-stranded Phenylalanine Zippers… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GUV
- Type
- protein
- Length
- 280 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.4
- Source
- Escherichia coli
- Molecule
- Major outer membrane lipoprotein
- UniProt
- P69776
- Pockets
- 1 · best druggability 0.68
Structure
x-ray diffraction · resolution 1.4 · 1 distinct chain · 93% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Major outer membrane lipoprotein | protein | 56 | 93% helix, 0% strand | P69776 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 84 | 0.68 | 0.91 | 20 | empty |
Interfaces
10 interfaces between chains.
- B–C · 1531 Ų buried · 17 hydrogen bonds · protein-protein
- A–E · 1498 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 1443 Ų buried · 20 hydrogen bonds · protein-protein
- D–E · 1431 Ų buried · 21 hydrogen bonds · protein-protein
- A–B · 1372 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 2GUV · Conformational transition between four- and five-stranded phenylalanine zippers… · the same entry in another collection · chain A against A, TM-score 1.00
- P69776 · AlphaFold monomer V2.0 prediction for major outer membrane lipoprotein lpp (P69776) · a predicted model of the same protein · chain A against A, TM-score 0.89
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 P69776
- Elsewhere: RCSB PDB 2GUV · PDBe 2GUV · UniProt P69776
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