Research workbench
TIR1-ASK1 complex structure
Analyse TIR1-ASK1 complex structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2P1M
- Type
- protein
- Length
- 657 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SKP1-like protein 1A; Transport inhibitor response 1 protein
- UniProt
- Q39255, Q570C0
- Ligands
- IHP
- Pockets
- 4 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SKP1-like protein 1A | protein | 90 | 60% helix, 0% strand | Q39255 |
| B | Transport inhibitor response 1 protein | protein | 567 | 38% helix, 19% strand | Q570C0 |
Ligands and binding sites
- IHP · Inositol hexakisphosphate · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 677 | 0.71 | 0.78 | 84 | IHP |
| 2 | 152 | 0.45 | 0.76 | 27 | empty |
| 3 | 86 | 0.41 | 0.78 | 16 | empty |
| 4 | 61 | 0.33 | 0.77 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1615 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 2P1M · TIR1-ASK1 complex structure · the same entry in another collection · chain A against A, TM-score 1.00
- Q570C0 · AlphaFold monomer V2.0 prediction for protein transport inhibitor response 1 (Q570C0) · a predicted model of the same protein · chain B against A, TM-score 0.99
- Q39255 · AlphaFold monomer V2.0 prediction for SKP1-like protein 1A (Q39255) · a predicted model of the same protein · chain A against A, TM-score 0.90
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 Q39255
- Every structure of UniProt Q570C0
- Elsewhere: RCSB PDB 2P1M · PDBe 2P1M · UniProt Q39255 · UniProt Q570C0
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