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Crystal structure of limulus polyphemus sap

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

PDB
1QTJ
Type
protein
Length
434 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (serum amyloid P component)
Pockets
7 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 47% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BProtein (serum amyloid P component)protein2176% helix, 47% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110810.840.85119empty
29810.830.85117empty
310570.780.80136empty
4600.350.7818empty
5870.340.7424empty

Interfaces

1 interface between chains.

  • A–B · 155 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 1QTJ · Crystal structure of limulus polyphemus sap · the same entry in another collection · chain A against A, TM-score 1.00

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