Research workbench
AlphaFold monomer V2.0 prediction for terminal nucleotidyltransferase 5A (Q96IP4)
Analyse AlphaFold monomer V2.0 prediction for terminal nucleotidyltransferase 5A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q96IP4
- Type
- protein
- Length
- 442 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xD0cfbEc245A8BAC2A6eE43DE22b2C650C2c695B5
- Molecule
- Terminal nucleotidyltransferase 5A
- UniProt
- Q96IP4
- Pockets
- 2 · best druggability 0.74
Structure
1 distinct chain · 39% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Terminal nucleotidyltransferase 5A | protein | 442 | 39% helix, 14% strand | Q96IP4 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 808 | 0.74 | 0.79 | 57 | empty |
| 2 | 146 | 0.44 | 0.76 | 21 | empty |
Compared structures
- 8EXF · Crystal structure of human FAM46A-BCCIPa complex at 3.2 angstrom resolution · an experimental structure of the same protein · chain A against A, TM-score 0.67
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 Q96IP4
- Elsewhere: UniProt Q96IP4 · AlphaFold DB Q96IP4
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