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Crystal structure of the computationally designed CAKE10 protein

Analyse Crystal structure of the computationally designed CAKE10 protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6TJI
Type
protein
Length
720 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
CAKE10
Ligands
PO4
Pockets
5 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 43% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BCAKE10protein3600% helix, 43% strand—

Ligands and binding sites

  • PO4 · Phosphate ion · ion · 6 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15200.590.7430empty
24070.540.7329empty
31590.480.7728empty
41520.460.7623empty
5620.440.8320empty

Interfaces

1 interface between chains.

  • A–B · 537 Ų buried · 13 hydrogen bonds · protein-protein

Compared structures

  • 6TJI · Crystal structure of the computationally designed Cake10 protein · the same entry in another collection · chain A against A, TM-score 1.00

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