Research workbench
AlphaFold monomer V2.0 prediction for thrombospondin-2 (P35442)
Analyse AlphaFold monomer V2.0 prediction for thrombospondin-2 (P35442) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P35442
- Type
- protein
- Length
- 1,172 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc0F878C3f3E2a1874e2A6daC80d429e553DdB0D5
- Molecule
- Thrombospondin-2
- UniProt
- P35442
- Pockets
- 7 · best druggability 0.79
Structure
1 distinct chain · 9% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thrombospondin-2 | protein | 1172 | 9% helix, 27% strand | P35442 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1025 | 0.79 | 0.81 | 96 | empty |
| 2 | 140 | 0.52 | 0.81 | 29 | empty |
| 3 | 164 | 0.47 | 0.77 | 30 | empty |
| 4 | 85 | 0.35 | 0.76 | 17 | empty |
| 5 | 56 | 0.32 | 0.77 | 13 | empty |
Modifications
Observed in the structure: 33 disulfide (disulfide).
Compared structures
- 2RHP · The thrombospondin-1 polymorphism ASN700SER associated with cornoary artery disease… · an experimental structure of the same protein · chain A against A, TM-score 0.53
- 2RHP · The Thrombospondin-1 Polymorphism Asn700Ser Associated with Cornoary Artery Disease… · an experimental structure of the same protein · chain A against A, TM-score 0.53
- 1YO8 · Structure of the C-terminal domain of human thrombospondin-2 · an experimental structure of the same protein · chain A against A, TM-score 0.53
- 1YO8 · Structure of the C-terminal domain of human thrombospondin-2 · an experimental structure of the same protein · chain A against A, TM-score 0.53
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 P35442
- Elsewhere: UniProt P35442 · AlphaFold DB P35442
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