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Structure of dodecameric unphosphorylated pediculus humanus (pH) PINK1 D357A mutant

Analyse Structure of dodecameric unphosphorylated pediculus humanus (pH) PINK1 D357A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7T4M
Type
protein
Length
4,854 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
SERINE/THREONINE-protein kinase PINK1, putative
EC
2.7.11.1
UniProt
E0W1I1
Pockets
20 · best druggability 0.82

Structure

electron microscopy · 2 distinct chains · 39% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, E, G, I, KSERINE/THREONINE-protein kinase PINK1, putative (EC 2.7.11.1)protein40839% helix, 14% strandE0W1I1
B, D, F, H, J, LSERINE/THREONINE-protein kinase PINK1, putative (EC 2.7.11.1)protein40139% helix, 15% strandE0W1I1

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110310.820.83117empty
210200.810.8293empty
310360.810.8283empty
410360.810.8297empty
510150.810.8292empty

Interfaces

24 interfaces between chains.

  • G–H · 1754 Ų buried · 31 hydrogen bonds · protein-protein
  • E–F · 1753 Ų buried · 30 hydrogen bonds · protein-protein
  • I–J · 1750 Ų buried · 30 hydrogen bonds · protein-protein
  • A–B · 1749 Ų buried · 30 hydrogen bonds · protein-protein
  • C–D · 1748 Ų buried · 29 hydrogen bonds · protein-protein

Compared structures

  • 7T4M · Structure of dodecameric unphosphorylated Pediculus humanus (Ph) PINK1 D357A mutant · the same entry in another collection · chain A against A, TM-score 1.00

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