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Crystal structure of signalling protein from SHEEP(SPS-40) at 3.0A resolution using crystal grown in the presence of polysaccharides

Analyse Crystal structure of signalling protein from SHEEP(SPS-40) at 3.0A resolution… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1SR0
Type
protein
Length
361 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Signal processing protein
Ligands
BMA, NAG, NDG
Pockets
3 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASignal processing proteinprotein36135% helix, 24% strand—

Ligands and binding sites

  • BMA · beta-D-mannopyranose · sugar · 3 copies
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
  • NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12290.550.7732empty
21820.550.7925empty
3960.390.7616empty

Modifications

Observed in the structure: 2 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

  • 1SR0 · Crystal structure of signalling protein from sheep(SPS-40) at 3.0A resolution using… · the same entry in another collection · chain A against A, TM-score 1.00

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