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The polyserine tract of nasonia vitripennis vg residues 351-385

Analyse The polyserine tract of nasonia vitripennis vg residues 351-385 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2LID
Type
protein
Length
35 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Vitellogenin

Structure

solution nmr · 1 distinct chain · 11% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AVitellogeninprotein3511% helix, 0% strand—

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

  • 2LID · The polyserine tract of Nasonia vitripennis Vg residues 351-385 · the same entry in another collection · chain A against A, TM-score 1.00

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