Research workbench
Crystal structure of SNX11/SNX10-pxe chimera
Analyse Crystal structure of SNX11/SNX10-pxe chimera in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KOK
- Type
- protein
- Length
- 295 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sorting nexin-11,UNCHARACTERIZED protein SNX10
- UniProt
- Q9Y5W9, Q75MY3
- Ligands
- NA, CL
- Pockets
- 2 · best druggability 0.48
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sorting nexin-11,UNCHARACTERIZED protein SNX10 | protein | 152 | 39% helix, 18% strand | Q9Y5W9, Q75MY3 |
| B | Sorting nexin-11,UNCHARACTERIZED protein SNX10 | protein | 143 | 43% helix, 20% strand | Q9Y5W9, Q75MY3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 110 | 0.48 | 0.80 | 20 | CL |
| 2 | 84 | 0.41 | 0.78 | 15 | CL |
Compared structures
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 Q9Y5W9
- Every structure of UniProt Q75MY3
- Elsewhere: RCSB PDB 6KOK · PDBe 6KOK · UniProt Q9Y5W9 · UniProt Q75MY3
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