MolNFT v1 · #469209 · protein
AlphaFold monomer V2.0 prediction for transposase for transposon TN4430 (P10021)
P10021: “AlphaFold monomer V2.0 prediction for transposase for transposon TN4430 (P10021)”. 11 pockets (best druggability 0.75). MolNFT v1 #469209 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P10021
- Type
- protein
- Length
- 987 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x41DAc1610BdbAC0b3d8730e65e31b2a34f5a1627
- Molecule
- Transposase for transposon TN4430
- UniProt
- P10021
- Pockets
- 11 · best druggability 0.75
Structure
1 distinct chain · 62% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transposase for transposon TN4430 | protein | 987 | 62% helix, 7% strand | P10021 |
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 477 | 0.75 | 0.83 | 67 | empty |
| 2 | 351 | 0.71 | 0.83 | 34 | empty |
| 3 | 469 | 0.60 | 0.75 | 56 | empty |
| 4 | 148 | 0.52 | 0.80 | 15 | empty |
| 5 | 175 | 0.43 | 0.74 | 27 | empty |
Compared structures
- 7QD4 · Cryo-EM structure of Tn4430 TnpA transposase from Tn3 family in complex with 100 bp long… · an experimental structure of the same protein · chain A against D, TM-score 0.80
- 7QD6 · Cryo-EM structure of Tn4430 TnpA transposase from Tn3 family in complex with… · an experimental structure of the same protein · chain A against A, TM-score 0.80
- 7QD5 · Cryo-EM structure of Tn4430 TnpA transposase from Tn3 family in complex with 48 bp long… · an experimental structure of the same protein · chain A against D, TM-score 0.79
- 7QD8 · Cryo-EM structure of Tn4430 TnpA transposase from Tn3 family in apo state · an experimental structure of the same protein · chain A against B, TM-score 0.64
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 P10021
- Elsewhere: UniProt P10021 · AlphaFold DB P10021
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