Research workbench
Solution NMR structure of BFR322 from bacteroides fragilis, northeast structural genomics consortium target BFR322
Analyse Solution NMR structure of BFR322 from bacteroides fragilis, northeast… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LIO
- Type
- protein
- Length
- 136 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- Q64YT5
- Pockets
- 1 · best druggability 0.76
Structure
solution nmr · 1 distinct chain · 24% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 136 | 24% helix, 38% strand | Q64YT5 |
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 | 644 | 0.76 | 0.81 | 43 | empty |
Compared structures
- 2LIO · Solution NMR Structure of BfR322 from Bacteroides fragilis, Northeast Structural Genomics… · the same entry in another collection · chain A against A, 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 Q64YT5
- Elsewhere: RCSB PDB 2LIO · PDBe 2LIO · UniProt Q64YT5
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