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Structure of a sting-associated cdne C-di-gmp synthase from flavobacteriaceae sp.

Analyse Structure of a sting-associated cdne C-di-gmp synthase from flavobacteriaceae… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6WT8
Type
protein
Length
356 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Sting-associated cdne C-di-gmp synthase
Pockets
4 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASting-associated cdne C-di-gmp synthaseprotein35656% helix, 13% strand—

Pockets

4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14060.620.7740empty
21920.480.7626empty
3720.400.7915empty
4530.330.7714empty

Modifications

Observed in the structure: 7 modified (engineered).

Compared structures

  • 6WT8 · Structure of a STING-associated CdnE c-di-GMP synthase from Flavobacteriaceae sp. · the same entry in another collection · chain A against A, TM-score 1.00

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