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Structure of apo vcp hexamer generated from bacterially recombinant VCP/P97

Analyse Structure of apo vcp hexamer generated from bacterially recombinant VCP/P97 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7K59
Type
protein
Length
4,446 residues
Chains
6
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 0.81

Structure

electron microscopy · 1 distinct chain · 34% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FTransitional endoplasmic reticulum ATPase (EC 3.6.4.6)protein74134% helix, 13% strandP55072

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110520.810.82100empty
27320.800.8481empty
37190.800.8489empty
46700.790.8485empty
55890.780.8473empty

Interfaces

6 interfaces between chains.

  • D–E · 3316 Ų buried · 22 hydrogen bonds · protein-protein
  • A–F · 3276 Ų buried · 20 hydrogen bonds · protein-protein
  • A–B · 3268 Ų buried · 19 hydrogen bonds · protein-protein
  • C–D · 3248 Ų buried · 17 hydrogen bonds · protein-protein
  • B–C · 3238 Ų buried · 18 hydrogen bonds · protein-protein

Compared structures

  • 7K59 · Structure of apo VCP hexamer generated from bacterially recombinant VCP/p97 · the same entry in another collection · chain A against A, TM-score 1.00

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