Research workbench
Mutant F105L of recombinant beta-lactoglobulin
Analyse Mutant F105L of recombinant beta-lactoglobulin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BGX
- Type
- protein
- Length
- 155 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Bos taurus
- Molecule
- Beta-lactoglobulin
- UniProt
- P02754
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · resolution 2 · 1 distinct chain · 17% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| AAA | Beta-lactoglobulin | protein | 155 | 17% helix, 44% strand | P02754 |
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 | 179 | 0.65 | 0.85 | 25 | GOL |
| 2 | 58 | 0.31 | 0.76 | 13 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- P02754 · AlphaFold monomer V2.0 prediction for beta-lactoglobulin (P02754) · a predicted model of the same protein · chain AAA against A, TM-score 0.97
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 P02754
- Elsewhere: RCSB PDB 7BGX · PDBe 7BGX · UniProt P02754
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