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Crystal structure of FEM1B
Analyse Crystal structure of FEM1B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LBF
- Type
- protein
- Length
- 685 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.252
- Source
- Homo sapiens
- Molecule
- Protein fem-1 homolog B
- UniProt
- Q9UK73
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · resolution 3.252 · 2 distinct chains · 52% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein fem-1 homolog B | protein | 343 | 52% helix, 5% strand | Q9UK73 |
| B | Protein fem-1 homolog B | protein | 342 | 51% helix, 5% strand | Q9UK73 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 631 | 0.68 | 0.76 | 61 | empty |
| 2 | 440 | 0.65 | 0.78 | 46 | empty |
Interfaces
1 interface between chains.
- A–B · 960 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
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 Q9UK73
- Elsewhere: RCSB PDB 6LBF · PDBe 6LBF · UniProt Q9UK73
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