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Cryo-EM structure of sulfolobus solfataricus ketol-acid reductoisomerase (sso-kari) with MG2+ at PH8.5

Analyse Cryo-EM structure of sulfolobus solfataricus ketol-acid reductoisomerase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6JCW
Type
protein
Length
3,912 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ketol-acid reductoisomerase
UniProt
Q97YJ9
Ligands
MG
Pockets
20 · best druggability 0.78

Structure

electron microscopy · 1 distinct chain · 48% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, LKetol-acid reductoisomeraseprotein32648% helix, 12% strandQ97YJ9

Ligands and binding sites

  • MG · Magnesium ion · metal · 24 copies · chains A, B, C, D, E, F, G, H, I, J, K, L

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19150.780.8074MG
29330.770.8079MG
38930.770.8064MG
49110.770.8078MG
58830.770.8074MG

Interfaces

30 interfaces between chains.

  • E–F · 5676 Ų buried · 28 hydrogen bonds · protein-protein
  • A–B · 5667 Ų buried · 28 hydrogen bonds · protein-protein
  • K–L · 5666 Ų buried · 29 hydrogen bonds · protein-protein
  • C–D · 5664 Ų buried · 29 hydrogen bonds · protein-protein
  • G–H · 5663 Ų buried · 30 hydrogen bonds · protein-protein

Compared structures

  • 6JCW · Cryo-EM Structure of Sulfolobus solfataricus ketol-acid reductoisomerase (Sso-KARI) with… · the same entry in another collection · chain L against L, TM-score 1.00

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