Research workbench
AlphaFold monomer V2.0 prediction for penicillin-binding protein 1A (Q9PGD4)
Analyse AlphaFold monomer V2.0 prediction for penicillin-binding protein 1A (Q9PGD4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9PGD4
- Type
- protein
- Length
- 809 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4F68597e66577F2Fc83E62a655Df07e7Ca4F542e
- Molecule
- Penicillin-binding protein 1A
- UniProt
- Q9PGD4
- Pockets
- 7 · best druggability 0.68
Structure
1 distinct chain · 40% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Penicillin-binding protein 1A | protein | 809 | 40% helix, 16% strand | Q9PGD4 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 471 | 0.68 | 0.79 | 45 | empty |
| 2 | 422 | 0.61 | 0.76 | 49 | empty |
| 3 | 197 | 0.55 | 0.79 | 30 | empty |
| 4 | 254 | 0.49 | 0.74 | 32 | empty |
| 5 | 230 | 0.48 | 0.74 | 24 | 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 Q9PGD4
- Elsewhere: UniProt Q9PGD4 · AlphaFold DB Q9PGD4
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