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Cryoem reconstruction of escrt-III filament composed of IST1 ntd R16E K27E double mutant

Analyse Cryoem reconstruction of escrt-III filament composed of IST1 ntd R16E K27E… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6TZA
Type
protein
Length
2,534 residues
Chains
14
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
IST1 homolog
UniProt
P53990
Pockets
20 · best druggability 0.80

Structure

electron microscopy · 1 distinct chain · 77% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, NIST1 homologprotein18177% helix, 0% strandP53990

Pockets

20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13080.800.9045empty
24270.780.8662empty
34760.770.8567empty
48070.770.80105empty
54860.760.8464empty

Interfaces

16 interfaces between chains.

  • C–J · 406 Ų buried · 1 hydrogen bond · protein-protein
  • D–E · 405 Ų buried · 2 hydrogen bonds · protein-protein
  • G–L · 399 Ų buried · 0 hydrogen bonds · protein-protein
  • C–M · 391 Ų buried · 0 hydrogen bonds · protein-protein
  • K–M · 390 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 6TZA · CryoEM reconstruction of ESCRT-III filament composed of IST1 NTD R16E K27E double mutant · the same entry in another collection · chain A against A, TM-score 1.00

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