Research workbench
High resolution structure of the major periplasmic domain from the cell shape-determining filament mrec (orthorhombic form)
Analyse High resolution structure of the major periplasmic domain from the cell… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QF4
- Type
- protein
- Length
- 337 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell shape determining protein mrec
- UniProt
- Q8DMY2
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 3% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell shape determining protein mrec | protein | 170 | 2% helix, 51% strand | Q8DMY2 |
| B | Cell shape determining protein mrec | protein | 167 | 4% helix, 51% strand | Q8DMY2 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 489 | 0.66 | 0.77 | 41 | EDO |
| 2 | 61 | 0.38 | 0.79 | 20 | empty |
| 3 | 100 | 0.37 | 0.75 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 510 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 2QF4 · High resolution structure of the major periplasmic domain from the cell shape-determining… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8DMY2 · AlphaFold monomer V2.0 prediction for cell shape-determining protein mrec (Q8DMY2) · a predicted model of the same protein · chain B against A, TM-score 0.92
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 Q8DMY2
- Elsewhere: RCSB PDB 2QF4 · PDBe 2QF4 · UniProt Q8DMY2
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