Research workbench
AlphaFold monomer V2.0 prediction for major cell-surface adhesin pac (P11657)
Analyse AlphaFold monomer V2.0 prediction for major cell-surface adhesin pac (P11657) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P11657
- Type
- protein
- Length
- 1,565 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x2E7853F600caf0B93109Bd82A4F48D84b36cE0c4
- Molecule
- Major cell-surface adhesin pac
- UniProt
- P11657
- Pockets
- 6 · best druggability 0.65
Structure
1 distinct chain · 31% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Major cell-surface adhesin pac | protein | 1565 | 31% helix, 23% strand | P11657 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 423 | 0.65 | 0.78 | 41 | empty |
| 2 | 292 | 0.54 | 0.75 | 38 | empty |
| 3 | 242 | 0.48 | 0.74 | 40 | empty |
| 4 | 130 | 0.38 | 0.73 | 21 | empty |
| 5 | 62 | 0.35 | 0.78 | 13 | empty |
Compared structures
- 3QE5 · Complete structure of Streptococcus mutans Antigen I/II carboxy-terminus · an experimental structure of the same protein · chain A against A, TM-score 0.31
- 3QE5 · Complete structure of streptococcus mutans antigen I/II carboxy- terminus · an experimental structure of the same protein · chain A against A, TM-score 0.31
- 1JMM · Crystal structure of the V-region of Streptococcus mutans antigen I/II · an experimental structure of the same protein · chain A against A, TM-score 0.24
- 1JMM · Crystal structure of the V-region of streptococcus mutans antigen I/II · an experimental structure of the same protein · chain A against A, TM-score 0.24
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 P11657
- Elsewhere: UniProt P11657 · AlphaFold DB P11657
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