Research workbench
Three-dimensional structure of human NLRP10/PYNOD pyrin domain
Analyse Three-dimensional structure of human NLRP10/PYNOD pyrin domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2M5V
- Type
- protein
- Length
- 102 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nacht, lrr and pyd domains-containing protein 10
- UniProt
- Q86W26
- Pockets
- 2 · best druggability 0.51
Structure
solution nmr · 1 distinct chain · 65% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nacht, lrr and pyd domains-containing protein 10 | protein | 102 | 65% helix, 0% strand | Q86W26 |
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 | 59 | 0.51 | 0.86 | 21 | empty |
| 2 | 76 | 0.44 | 0.80 | 16 | empty |
Compared structures
- 2M5V · Three-dimensional structure of human NLRP10/PYNOD pyrin domain · the same entry in another collection · chain A against A, TM-score 1.00
- Q86W26 · AlphaFold monomer V2.0 prediction for nacht, lrr and pyd domains- containing protein 10… · 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 Q86W26
- Elsewhere: RCSB PDB 2M5V · PDBe 2M5V · UniProt Q86W26
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