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Structure of vcp dodecamer purified from H1299 cells

Analyse Structure of vcp dodecamer purified from H1299 cells in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7K56
Type
protein
Length
8,892 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transitional endoplasmic reticulum ATPase
EC
3.6.4.6
UniProt
P55072
Pockets
20 · best druggability 0.84

Structure

electron microscopy · 1 distinct chain · 35% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, LTransitional endoplasmic reticulum ATPase (EC 3.6.4.6)protein74135% helix, 12% strandP55072

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110610.840.85128empty
211530.840.85153empty
39380.840.85121empty
49270.840.85118empty
59410.830.85124empty

Interfaces

24 interfaces between chains.

  • A–B · 3625 Ų buried · 28 hydrogen bonds · protein-protein
  • B–C · 3624 Ų buried · 27 hydrogen bonds · protein-protein
  • G–L · 3619 Ų buried · 27 hydrogen bonds · protein-protein
  • A–F · 3619 Ų buried · 27 hydrogen bonds · protein-protein
  • J–K · 3619 Ų buried · 26 hydrogen bonds · protein-protein

Compared structures

  • 7K56 · Structure of VCP dodecamer purified from H1299 cells · the same entry in another collection · chain A against A, TM-score 1.00

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