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Structure of a fragment of human fibronectin containing the 10TH, 11TH and 12TH type III domains

Analyse Structure of a fragment of human fibronectin containing the 10TH, 11TH and 12TH… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6XAY
Type
protein
Length
1,084 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fibronectin
UniProt
P02751
Pockets
13 · best druggability 0.64

Structure

x-ray diffraction · 3 distinct chains · 0% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, DFibronectinprotein2720% helix, 52% strandP02751
BFibronectinprotein2690% helix, 54% strandP02751
CFibronectinprotein2710% helix, 48% strandP02751

Ligands and binding sites

  • GOL · Glycerol · additive · 6 copies · chains A, D, B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

13 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13460.640.8047empty
24710.630.7741empty
3760.630.9120empty
43360.630.7946empty
52040.620.8329empty

Interfaces

5 interfaces between chains.

  • A–D · 1861 Ų buried · 26 hydrogen bonds · protein-protein
  • B–C · 1850 Ų buried · 20 hydrogen bonds · protein-protein
  • A–B · 487 Ų buried · 5 hydrogen bonds · protein-protein
  • C–D · 484 Ų buried · 4 hydrogen bonds · protein-protein
  • B–D · 40 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 6XAY · Structure of a fragment of human fibronectin containing the 10th, 11th and 12th type III… · the same entry in another collection · chain D against D, TM-score 1.00
  • P02751 · AlphaFold monomer V2.0 prediction for fibronectin (P02751) · a predicted model of the same protein · chain C against A, TM-score 0.66

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