Research workbench
The crystal structure of the hypothetical protein NE1496
Analyse The crystal structure of the hypothetical protein NE1496 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FBL
- Type
- protein
- Length
- 292 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein NE1496
- Ligands
- NA
- Pockets
- 3 · best druggability 0.41
Structure
x-ray diffraction · 2 distinct chains · 19% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein NE1496 | protein | 144 | 20% helix, 44% strand | — |
| B | Hypothetical protein NE1496 | protein | 148 | 18% helix, 43% strand | — |
Ligands and binding sites
- NA · Sodium ion · metal · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 98 | 0.41 | 0.78 | 22 | empty |
| 2 | 99 | 0.40 | 0.77 | 24 | empty |
| 3 | 50 | 0.30 | 0.77 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 809 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 2FBL · The crystal structure of the hypothetical protein NE1496 · 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
- Elsewhere: RCSB PDB 2FBL · PDBe 2FBL
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