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Structural basis for the interactions between tenascins and the C-type lectin domains from lecticans: evidence for a cross-linking role for tenascins

Analyse Structural basis for the interactions between tenascins and the C-type lectin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1TDQ
Type
protein
Length
397 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
Q05546, P07897

Structure

x-ray diffraction · 2 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein271—Q05546
B—protein126—P07897

Compared structures

  • 1TDQ · Structural basis for the interactions between tenascins and the C-type lectin domains… · the same entry in another collection · chain A against A, TM-score 1.00
  • P07897 · AlphaFold monomer V2.0 prediction for aggrecan core protein (P07897) · a predicted model of the same protein · chain B against A, TM-score 0.97
  • Q05546 · AlphaFold monomer V2.0 prediction for tenascin-R (Q05546) · a predicted model of the same protein · chain A against A, TM-score 0.82

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