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Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences

Analyse Crystallographic analysis of oxygenated and deoxygenated states of arthropod… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1OXY
Type
protein
Length
573 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hemocyanin (subunit type II)
UniProt
P04253
Ligands
CU, OXY
Pockets
9 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHemocyanin (subunit type II)protein57336% helix, 19% strandP04253

Ligands and binding sites

  • CU · Copper (II) ion · metal · 2 copies · chains A
  • OXY · Oxygen molecule · ion · chains A

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

Pockets

9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11450.650.8731empty
22680.580.7836empty
32560.520.7541empty
4730.490.8325empty
51380.440.7616empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 1OXY · Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin… · the same entry in another collection · chain A against A, TM-score 1.00
  • P04253 · AlphaFold monomer V2.0 prediction for hemocyanin II (P04253) · a predicted model of the same protein · chain A against A, TM-score 1.00

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