Research workbench
AlphaFold monomer V2.0 prediction for pulmonary surfactant-associated protein B (P50405)
Analyse AlphaFold monomer V2.0 prediction for pulmonary surfactant-associated protein B… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P50405
- Type
- protein
- Length
- 377 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5C0bC9C36F16996167015afdB6C60c73a394D024
- Molecule
- Pulmonary surfactant-associated protein B
- UniProt
- P50405
- Pockets
- 2 · best druggability 0.39
Structure
1 distinct chain · 56% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pulmonary surfactant-associated protein B | protein | 377 | 56% helix, 0% strand | P50405 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 85 | 0.39 | 0.76 | 17 | empty |
| 2 | 101 | 0.37 | 0.74 | 17 | empty |
Modifications
Observed in the structure: 12 disulfide (disulfide).
Compared structures
- 6VZD · N-terminal domain of mouse surfactant protein B (K46E/R51E mutant) with bound lipid · an experimental structure of the same protein · chain A against E, TM-score 0.22
- 6VYN · N-terminal domain of mouse surfactant protein B with bound lipid, wild type · an experimental structure of the same protein · chain A against E, TM-score 0.21
- 6W1B · N-terminal domain of mouse surfactant protein B with bound lipid, Y59A/H79A mutant · an experimental structure of the same protein · chain A against C, TM-score 0.21
- 7MBK · N-terminal domain of mouse surfactant protein B, 6W mutant · an experimental structure of the same protein · chain A against B, TM-score 0.20
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 P50405
- Elsewhere: UniProt P50405 · AlphaFold DB P50405
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