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The high resolution structure of annexin III shows differences with annexin V

Analyse The high resolution structure of annexin III shows differences with annexin V in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1AXN
Type
protein
Length
323 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Annexin III
UniProt
P12429
Ligands
CA
Pockets
4 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 71% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAnnexin IIIprotein32371% helix, 0% strandP12429

Ligands and binding sites

  • CA · Calcium ion · metal · 5 copies · chains A

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1740.560.8825empty
22490.510.7527empty
31210.470.7920empty
4530.290.7511empty

Compared structures

  • 1AXN · The high resolution structure of annexin III shows differences with annexin V · the same entry in another collection · chain A against A, TM-score 1.00
  • P12429 · AlphaFold monomer V2.0 prediction for annexin A3 (P12429) · a predicted model of the same protein · chain A against A, TM-score 0.99

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