Research workbench
AlphaFold monomer V2.0 prediction for bifunctional polynucleotide PHOSPHATASE/KINASE (Q96T60)
Analyse AlphaFold monomer V2.0 prediction for bifunctional polynucleotide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q96T60
- Type
- protein
- Length
- 521 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0056155E6B76709C124E31067C4d1B97cA9dA71a
- Molecule
- Bifunctional polynucleotide PHOSPHATASE/KINASE
- UniProt
- Q96T60
- Pockets
- 6 · best druggability 0.69
Structure
1 distinct chain · 25% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional polynucleotide PHOSPHATASE/KINASE | protein | 521 | 25% helix, 20% strand | Q96T60 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 655 | 0.69 | 0.77 | 67 | empty |
| 2 | 195 | 0.66 | 0.85 | 28 | empty |
| 3 | 271 | 0.54 | 0.76 | 33 | empty |
| 4 | 143 | 0.42 | 0.75 | 20 | empty |
| 5 | 53 | 0.42 | 0.83 | 13 | empty |
Compared structures
- 2W3O · Crystal structure of the human PNKP FHA domain in complex with an XRCC1-derived… · an experimental structure of the same protein · chain A against B, TM-score 0.19
- 2W3O · Crystal structure of the human pnkp fha domain in complex with an XRCC1-derived… · an experimental structure of the same protein · chain A against B, TM-score 0.19
- 2BRF · Crystal Structure of the FHA Domain of Human Polynucleotide Kinase 3' Phosphatase · an experimental structure of the same protein · chain A against A, TM-score 0.19
- 2BRF · Crystal structure of the fha domain of human polynucleotide kinase 3' phosphatase · an experimental structure of the same protein · chain A against A, TM-score 0.19
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 Q96T60
- Elsewhere: UniProt Q96T60 · AlphaFold DB Q96T60
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