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Crystal structure of spop bound with a peptide

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

PDB
7D3D
Type
protein
Length
301 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Speckle-type poz protein; Glu-val-ser-ile-ile-gln-gly-ala-asp-ser-thr-thr
UniProt
O43791
Pockets
3 · best druggability 0.73

Structure

x-ray diffraction · 3 distinct chains · 13% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASpeckle-type poz proteinprotein13912% helix, 50% strandO43791
a, bGlu-val-ser-ile-ile-gln-gly-ala-asp-ser-thr-thrprotein120% helix, 42% strand—
BSpeckle-type poz proteinprotein13814% helix, 52% strandO43791

Ligands and binding sites

  • GOL · Glycerol · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15270.730.8156empty
21400.420.7525empty
3630.350.7714empty

Interfaces

4 interfaces between chains.

  • A–a · 688 Ų buried · 22 hydrogen bonds · protein-protein
  • B–b · 677 Ų buried · 24 hydrogen bonds · protein-protein
  • A–b · 454 Ų buried · 7 hydrogen bonds · protein-protein
  • A–B · 176 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 7D3D · Crystal structure of SPOP bound with a peptide · the same entry in another collection · chain A against A, TM-score 1.00
  • O43791 · AlphaFold monomer V2.0 prediction for speckle-type poz protein (O43791) · a predicted model of the same protein · chain A against A, TM-score 0.97

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