Research workbench
Crystal structure of programmed cell death 10 in complex with inositol 1,3,4,5-tetrakisphosphate
Analyse Crystal structure of programmed cell death 10 in complex with inositol… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3AJM
- Type
- protein
- Length
- 391 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Programmed cell death protein 10
- UniProt
- Q9BUL8
- Ligands
- 4IP
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 82% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Programmed cell death protein 10 | protein | 201 | 83% helix, 0% strand | Q9BUL8 |
| B | Programmed cell death protein 10 | protein | 190 | 81% helix, 0% strand | Q9BUL8 |
Ligands and binding sites
- 4IP · Inositol-(1,3,4,5)-tetrakisphosphate · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 435 | 0.70 | 0.81 | 39 | empty |
| 2 | 117 | 0.37 | 0.74 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1982 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 3AJM · Crystal structure of programmed cell death 10 in complex with inositol… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9BUL8 · AlphaFold monomer V2.0 prediction for programmed cell death protein 10 (Q9BUL8) · a predicted model of the same protein · chain A against A, TM-score 0.69
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 Q9BUL8
- Elsewhere: RCSB PDB 3AJM · PDBe 3AJM · UniProt Q9BUL8
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