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Rabbit muscle aldolase determined using single-particle cryo-EM at 200 keV

Analyse Rabbit muscle aldolase determined using single-particle cryo-EM at 200 keV in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6V20
Type
protein
Length
1,372 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.13
Source
Oryctolagus cuniculus
Molecule
Fructose-bisphosphate aldolase A
EC
4.1.2.13
UniProt
P00883
Pockets
14 · best druggability 0.88

Structure

electron microscopy · resolution 2.13 · 1 distinct chain · 46% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DFructose-bisphosphate aldolase A (EC 4.1.2.13)protein34346% helix, 15% strandP00883

Pockets

14 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111540.880.89123empty
24940.820.8857empty
37430.800.8398empty
41750.670.8746empty
51610.660.8745empty

Interfaces

6 interfaces between chains.

  • A–C · 1273 Ų buried · 23 hydrogen bonds · protein-protein
  • B–D · 1273 Ų buried · 23 hydrogen bonds · protein-protein
  • A–B · 1180 Ų buried · 16 hydrogen bonds · protein-protein
  • C–D · 1179 Ų buried · 17 hydrogen bonds · protein-protein
  • B–C · 75 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 6V20 · Rabbit muscle aldolase determined using single-particle cryo-EM at 200 kev · the same entry in another collection · chain D against D, TM-score 1.00
  • P00883 · AlphaFold monomer V2.0 prediction for fructose-bisphosphate aldolase a (P00883) · a predicted model of the same protein · chain C against A, TM-score 1.00

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