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Annexin XII E105K homohexamer crystal structure

Analyse Annexin XII E105K homohexamer crystal structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1DM5
Type
protein
Length
1,890 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Annexin XII E105K mutant homohexamer
UniProt
P26256
Ligands
CA
Pockets
20 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 73% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FAnnexin XII E105K mutant homohexamerprotein31573% helix, 0% strandP26256

Ligands and binding sites

  • CA · Calcium ion · metal · 11 copies · chains A, E, B, D, C, F

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19900.790.81102CA
29750.780.8197CA
37510.770.8265empty
48970.770.8097empty
59310.760.7981empty

Interfaces

12 interfaces between chains.

  • A–E · 1071 Ų buried · 17 hydrogen bonds · protein-protein
  • B–D · 1066 Ų buried · 17 hydrogen bonds · protein-protein
  • C–F · 1042 Ų buried · 16 hydrogen bonds · protein-protein
  • A–C · 680 Ų buried · 13 hydrogen bonds · protein-protein
  • D–F · 649 Ų buried · 15 hydrogen bonds · protein-protein

Compared structures

  • 1DM5 · Annexin XII E105K homohexamer crystal structure · the same entry in another collection · chain F against F, TM-score 1.00
  • P26256 · AlphaFold monomer V2.0 prediction for annexin-B12 (P26256) · a predicted model of the same protein · chain A against A, TM-score 1.00

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