Research workbench
Structure of the tandem SH2 domains from antonospora locustae transcription elongation factor SPT6
Analyse Structure of the tandem SH2 domains from antonospora locustae transcription… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XP1
- Type
- protein
- Length
- 175 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SPT6
- Ligands
- SO4, CL
- Pockets
- 1 · best druggability 0.41
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SPT6 | protein | 175 | 28% helix, 34% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 78 | 0.41 | 0.79 | 19 | empty |
Compared structures
- 2XP1 · Structure of the tandem SH2 domains from Antonospora locustae transcription elongation… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 2XP1 · PDBe 2XP1
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