Research workbench
Structure of SNX27 FERM complexed with Fam21A repeat 15 (1124-1140)
Analyse Structure of SNX27 FERM complexed with Fam21A repeat 15 (1124-1140) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8TTT
- Type
- protein
- Length
- 262 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.35
- Source
- Homo sapiens; SYNTHETIC CONSTRUCT
- Molecule
- Sorting nexin-27; Fam21A repeat 15 peptide
- UniProt
- Q96L92, Q641Q2
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · resolution 2.35 · 2 distinct chains · 32% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sorting nexin-27 | protein | 256 | 32% helix, 29% strand | Q96L92 |
| B | Fam21A repeat 15 peptide | protein | 6 | 0% helix, 0% strand | Q641Q2 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 277 | 0.69 | 0.84 | 47 | GOL |
| 2 | 159 | 0.40 | 0.73 | 35 | empty |
| 3 | 66 | 0.32 | 0.76 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 391 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- Q96L92 · AlphaFold monomer V2.0 prediction for sorting nexin-27 (Q96L92) · a predicted model of the same protein · chain A against A, TM-score 0.96
- Q641Q2 · AlphaFold monomer V2.0 prediction for wash complex subunit 2A (Q641Q2) · a predicted model of the same protein · chain B against A, TM-score 0.64
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 Q96L92
- Every structure of UniProt Q641Q2
- Elsewhere: RCSB PDB 8TTT · PDBe 8TTT · UniProt Q96L92 · UniProt Q641Q2
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