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Structure of rhodothermus marinus cdne C-ump-AMP synthase

Analyse Structure of rhodothermus marinus cdne C-ump-AMP synthase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6E0K
Type
protein
Length
295 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
CGAS/DNCV-like nucleotidyltransferase in E. COLI homolog
UniProt
G2SLH8
Pockets
2 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACGAS/DNCV-like nucleotidyltransferase in E. COLI homologprotein29544% helix, 18% strandG2SLH8

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14510.610.7643empty
2930.370.7515empty

Compared structures

  • 6E0K · Structure of Rhodothermus marinus CdnE c-UMP-AMP synthase · the same entry in another collection · chain A against A, TM-score 1.00
  • G2SLH8 · AlphaFold monomer V2.0 prediction for cyclic ump-AMP synthase (G2SLH8) · a predicted model of the same protein · chain A against A, TM-score 0.94

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