Research workbench
Crystal structure of sek
Analyse Crystal structure of sek in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NTT
- Type
- protein
- Length
- 434 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Staphylococcal enterotoxin K
- UniProt
- Q5HHK0
- Ligands
- CL
- Pockets
- 5 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Staphylococcal enterotoxin K | protein | 217 | 21% helix, 38% strand | Q5HHK0 |
Ligands and binding sites
- CL · Chloride ion · ion · 13 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 10 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.45 | 0.82 | 14 | CL |
| 2 | 110 | 0.42 | 0.77 | 22 | empty |
| 3 | 58 | 0.35 | 0.78 | 14 | CL |
| 4 | 90 | 0.32 | 0.73 | 20 | CL |
| 5 | 54 | 0.31 | 0.76 | 22 | EDO |
Interfaces
1 interface between chains.
- A–B · 563 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 2NTT · Crystal Structure of SEK · the same entry in another collection · chain A against A, TM-score 1.00
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 Q5HHK0
- Elsewhere: RCSB PDB 2NTT · PDBe 2NTT · UniProt Q5HHK0
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