Research workbench
NMR structure of BEF3 activated SMA0114
Analyse NMR structure of BEF3 activated SMA0114 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2M98
- Type
- protein
- Length
- 123 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Two-component response regulator
- UniProt
- Q930Y6
- Ligands
- BEF, CA
- Pockets
- 2 · best druggability 0.57
Structure
solution nmr · 1 distinct chain · 32% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Two-component response regulator | protein | 123 | 32% helix, 9% strand | Q930Y6 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 143 | 0.57 | 0.83 | 38 | empty |
| 2 | 61 | 0.44 | 0.82 | 16 | empty |
Compared structures
- 2M98 · NMR Structure of BeF3 Activated Sma0114 · 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 Q930Y6
- Elsewhere: RCSB PDB 2M98 · PDBe 2M98 · UniProt Q930Y6
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