Research workbench
Crystal structure of the pgm domain of the suppressor of T-cell receptor (sts-1)
Analyse Crystal structure of the pgm domain of the suppressor of T-cell receptor (sts-1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2H0Q
- Type
- protein
- Length
- 778 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Suppressor of T-cell receptor signaling 1
- UniProt
- Q8BGG7
- Pockets
- 9 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Suppressor of T-cell receptor signaling 1 | protein | 261 | 37% helix, 13% strand | Q8BGG7 |
| B | Suppressor of T-cell receptor signaling 1 | protein | 256 | 36% helix, 13% strand | Q8BGG7 |
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1103 | 0.80 | 0.81 | 84 | empty |
| 2 | 265 | 0.57 | 0.78 | 40 | empty |
| 3 | 154 | 0.55 | 0.81 | 27 | empty |
| 4 | 194 | 0.48 | 0.75 | 26 | empty |
| 5 | 150 | 0.47 | 0.77 | 27 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1657 Ų buried · 30 hydrogen bonds · protein-protein
- B–C · 580 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 391 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2H0Q · Crystal Structure of the PGM domain of the Suppressor of T-Cell receptor (Sts-1) · the same entry in another collection · chain A against A, TM-score 1.00
- Q8BGG7 · AlphaFold monomer V2.0 prediction for ubiquitin-associated and SH3 domain-containing… · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q8BGG7
- Elsewhere: RCSB PDB 2H0Q · PDBe 2H0Q · UniProt Q8BGG7
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