Research workbench
NMR structure determination of the periplasmic domain of exbd from E.COLI
Analyse NMR structure determination of the periplasmic domain of exbd from E.COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PFU
- Type
- protein
- Length
- 99 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Biopolymer transport exbd protein
- UniProt
- P0ABV2
- Pockets
- 2 · best druggability 0.42
Structure
solution nmr · 1 distinct chain · 21% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Biopolymer transport exbd protein | protein | 99 | 21% helix, 19% strand | P0ABV2 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 95 | 0.42 | 0.78 | 23 | empty |
| 2 | 51 | 0.41 | 0.82 | 13 | empty |
Compared structures
- 2PFU · NMR structure determination of the periplasmic domain of ExbD from E.coli · the same entry in another collection · chain A against A, TM-score 1.00
- P0ABV2 · AlphaFold monomer V2.0 prediction for biopolymer transport protein exbd (P0ABV2) · a predicted model of the same protein · chain A against A, TM-score 0.65
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 P0ABV2
- Elsewhere: RCSB PDB 2PFU · PDBe 2PFU · UniProt P0ABV2
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