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DHD15_CLOSED

Analyse DHD15_CLOSED in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6DMA
Type
protein
Length
560 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
DHD15_CLOSED_A; DHD15_CLOSED_B
Pockets
11 · best druggability 0.73

Structure

x-ray diffraction · 8 distinct chains · 93% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADHD15_CLOSED_Aprotein7194% helix, 0% strand—
BDHD15_CLOSED_Bprotein7486% helix, 0% strand—
CDHD15_CLOSED_Aprotein7390% helix, 0% strand—
DDHD15_CLOSED_Bprotein6894% helix, 0% strand—
EDHD15_CLOSED_Aprotein7194% helix, 0% strand—
FDHD15_CLOSED_Bprotein6994% helix, 0% strand—
GDHD15_CLOSED_Aprotein7194% helix, 0% strand—
HDHD15_CLOSED_Bprotein6392% helix, 0% strand—

Pockets

11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15010.730.8282empty
22100.610.8241empty
31250.600.8528empty
42290.590.8033empty
51540.580.8228empty

Interfaces

14 interfaces between chains.

  • A–B · 1239 Ų buried · 3 hydrogen bonds · protein-protein
  • C–D · 1066 Ų buried · 5 hydrogen bonds · protein-protein
  • E–F · 897 Ų buried · 1 hydrogen bond · protein-protein
  • G–H · 767 Ų buried · 0 hydrogen bonds · protein-protein
  • B–D · 237 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 6DMA · DHD15_closed · the same entry in another collection · chain A against A, TM-score 1.00

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