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Murine saposin-D (sapd), open conformation

Analyse Murine saposin-D (sapd), open conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5U85
Type
protein
Length
155 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Saposin-D
UniProt
Q61207
Pockets
1 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 79% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASaposin-Dprotein7877% helix, 0% strandQ61207
BSaposin-Dprotein7781% helix, 0% strandQ61207

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15660.810.8643empty

Interfaces

1 interface between chains.

  • A–B · 1517 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 5U85 · Murine saposin-D (SapD), open conformation · the same entry in another collection · chain A against A, TM-score 1.00
  • Q61207 · AlphaFold monomer V2.0 prediction for prosaposin (Q61207) · a predicted model of the same protein · chain A against A, TM-score 0.60

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