Research workbench
Crystal structure of the computationally designed CAKE3 protein
Analyse Crystal structure of the computationally designed CAKE3 protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TJC
- Type
- protein
- Length
- 360 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CAKE3
- Ligands
- PO4
- Pockets
- 1 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | CAKE3 | protein | 120 | 0% helix, 43% strand | — |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 4 copies · chains A, B, C
- GOL · Glycerol · additive · 4 copies · chains B, C, 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 477 | 0.57 | 0.73 | 27 | empty |
Interfaces
3 interfaces between chains.
- B–C · 992 Ų buried · 22 hydrogen bonds · protein-protein
- A–C · 972 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 963 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 6TJC · Crystal structure of the computationally designed Cake3 protein · 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
- Elsewhere: RCSB PDB 6TJC · PDBe 6TJC
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