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Cryo-EM structure of the desulfovibrio vulgaris type I-C apo cascade

Analyse Cryo-EM structure of the desulfovibrio vulgaris type I-C apo cascade in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7KHA
Type
protein + RNA
Length
2,892 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
CRISPR-associated protein, CT1134 family; CRISPR-associated protein, TM1801 family…
UniProt
Q72WF9, Q72WF7, Q72WF8
Pockets
20 · best druggability 0.87

Structure

electron microscopy · 5 distinct chains · 30% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACRISPR-associated protein, CT1134 familyprotein22010% helix, 26% strandQ72WF9
B, C, D, E, F, G, HCRISPR-associated protein, TM1801 familyprotein28626% helix, 27% strandQ72WF7
ICRISPR-associated protein, CT1133 familyprotein38537% helix, 7% strandQ72WF8
K, LCRISPR-associated protein, CT1133 familyprotein12058% helix, 0% strandQ72WF8
JRNA (45-mer)rna45——

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17710.870.90121empty
23370.800.9051empty
31270.770.9629empty
45970.760.8394empty
55780.760.8372empty

Interfaces

36 interfaces between chains.

  • A–B · 2435 Ų buried · 32 hydrogen bonds · protein-protein
  • F–G · 1728 Ų buried · 20 hydrogen bonds · protein-protein
  • G–H · 1721 Ų buried · 20 hydrogen bonds · protein-protein
  • B–C · 1711 Ų buried · 22 hydrogen bonds · protein-protein
  • C–D · 1691 Ų buried · 23 hydrogen bonds · protein-protein

Compared structures

  • 7KHA · Cryo-EM Structure of the Desulfovibrio vulgaris Type I-C Apo Cascade · the same entry in another collection · chain A against A, TM-score 1.00

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