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Crystal structure of dltd

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

PDB
7DXM
Type
protein
Length
1,564 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein dltd
UniProt
Q5M4V2
Ligands
SO4
Pockets
19 · best druggability 0.84

Structure

x-ray diffraction · 3 distinct chains · 53% helix, 7% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein dltdprotein39153% helix, 7% strandQ5M4V2
B, DProtein dltdprotein39254% helix, 7% strandQ5M4V2
CProtein dltdprotein38952% helix, 7% strandQ5M4V2

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 4 copies · chains A, B, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

19 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110410.840.8570empty
210140.830.84110SO4
36670.740.8151empty
42980.630.7937empty
5620.630.9320empty

Interfaces

4 interfaces between chains.

  • B–C · 1341 Ų buried · 13 hydrogen bonds · protein-protein
  • C–D · 851 Ų buried · 10 hydrogen bonds · protein-protein
  • A–B · 323 Ų buried · 4 hydrogen bonds · protein-protein
  • B–D · 180 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 7DXM · Crystal structure of DltD · the same entry in another collection · chain A against A, TM-score 1.00

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