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Cryo-EM structure of the drosophila CTP synthase substrate-bound filament

Analyse Cryo-EM structure of the drosophila CTP synthase substrate-bound filament in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6L6Z
Type
protein
Length
4,496 residues
Chains
8
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
CTP synthase
EC
6.3.4.2
UniProt
Q9VUL1
Pockets
20 · best druggability 0.86

Structure

electron microscopy · 1 distinct chain · 31% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
D, A, B, C, H, E, F, GCTP synthase (EC 6.3.4.2)protein56231% helix, 15% strandQ9VUL1

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16700.860.9196empty
23520.840.9377empty
34290.830.9066empty
410640.820.8393empty
52610.820.9337empty

Interfaces

16 interfaces between chains.

  • A–B · 1375 Ų buried · 9 hydrogen bonds · protein-protein
  • E–F · 1373 Ų buried · 8 hydrogen bonds · protein-protein
  • D–C · 1354 Ų buried · 9 hydrogen bonds · protein-protein
  • H–G · 1353 Ų buried · 9 hydrogen bonds · protein-protein
  • H–E · 1134 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 6L6Z · Cryo-EM structure of the Drosophila CTP synthase substrate-bound filament · the same entry in another collection · chain G against G, TM-score 1.00
  • Q9VUL1 · AlphaFold monomer V2.0 prediction for CTP synthase (Q9VUL1) · a predicted model of the same protein · chain D against A, TM-score 0.95

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