Research workbench
AlphaFold monomer V2.0 prediction for penicillin-binding protein 1A (Q92G78)
Analyse AlphaFold monomer V2.0 prediction for penicillin-binding protein 1A (Q92G78) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q92G78
- Type
- protein
- Length
- 790 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x661f92Fc5950020C7aB410B5F5b9a3f429F49Ae5
- Molecule
- Penicillin-binding protein 1A
- UniProt
- Q92G78
- Pockets
- 10 · best druggability 0.58
Structure
1 distinct chain · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Penicillin-binding protein 1A | protein | 790 | 43% helix, 16% strand | Q92G78 |
Pockets
10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 319 | 0.58 | 0.77 | 41 | empty |
| 2 | 257 | 0.58 | 0.78 | 34 | empty |
| 3 | 91 | 0.43 | 0.79 | 17 | empty |
| 4 | 124 | 0.36 | 0.73 | 20 | empty |
| 5 | 70 | 0.35 | 0.76 | 16 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q92G78
- Elsewhere: UniProt Q92G78 · AlphaFold DB Q92G78
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