Research workbench
Crystal structure of kibra and PTPN14 complex
Analyse Crystal structure of kibra and PTPN14 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6JJW
- Type
- protein
- Length
- 109 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein kibra; Peptide from tyrosine-protein phosphatase non-receptor type 14
- UniProt
- Q5SXA9, Q15678
- Ligands
- MG, CL
- Pockets
- 1 · best druggability 0.27
Structure
x-ray diffraction · 2 distinct chains · 19% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein kibra | protein | 89 | 16% helix, 31% strand | Q5SXA9 |
| U | Peptide from tyrosine-protein phosphatase non-receptor type 14 | protein | 20 | 35% helix, 0% strand | Q15678 |
Ligands and binding sites
- MG · Magnesium ion · metal
- CL · Chloride ion · ion · 8 copies · chains A, U
- FMT · Formic acid · additive · 3 copies · chains A, U
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 51 | 0.27 | 0.75 | 13 | empty |
Interfaces
1 interface between chains.
- A–U · 863 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 6JJW · Crystal Structure of KIBRA and PTPN14 complex · the same entry in another collection · chain U against U, TM-score 1.00
- Q5SXA9 · AlphaFold monomer V2.0 prediction for protein kibra (Q5SXA9) · a predicted model of the same protein · chain A against A, TM-score 0.51
- Q15678 · AlphaFold monomer V2.0 prediction for tyrosine-protein phosphatase non-receptor type 14… · a predicted model of the same protein · chain U against A, TM-score 0.33
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 Q5SXA9
- Every structure of UniProt Q15678
- Elsewhere: RCSB PDB 6JJW · PDBe 6JJW · UniProt Q5SXA9 · UniProt Q15678
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.