Hemocyanin

Hemocyanin, copper containing domain
Single oxygenated functional unit from the hemocyanin of an octopus
Identifiers
SymbolHemocyanin_M
PfamPF00372
InterProIPR000896
PROSITEPDOC00184
SCOP21lla / SCOPe / SUPFAM
Available protein structures:
PDB  1oxy :110-373 1nol :110-373 1lla :110-373

1ll1 :110-373 1hc1A:136-393 1hcyD:136-393 1hc6B:136-393 1hc4C:136-393 1hc3C:136-393 1hc5C:136-393 1hc2C:136-393 IPR000896 PF00372 (ECOD; PDBsum)

 
AlphaFold
Hemocyanin, all-alpha domain
Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 angstroms resolution
Identifiers
SymbolHemocyanin_N
PfamPF03722
InterProIPR005204
PROSITEPDOC00184
SCOP21lla / SCOPe / SUPFAM
Available protein structures:
PDB  IPR005204 PF03722 (ECOD; PDBsum)  
AlphaFold
Hemocyanin, ig-like domain
crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences
Identifiers
SymbolHemocyanin_C
PfamPF03723
InterProIPR005203
PROSITEPDOC00184
SCOP21lla / SCOPe / SUPFAM
Available protein structures:
PDB  IPR005203 PF03723 (ECOD; PDBsum)  
AlphaFold

Hemocyanins (also spelled haemocyanins and abbreviated Hc) are proteins that transport oxygen throughout the bodies of some invertebrate animals. These metalloproteins contain two copper atoms that reversibly bind a single oxygen molecule (O2). They are second only to hemoglobin in frequency of use as an oxygen transport molecule. Unlike the hemoglobin in red blood cells found in vertebrates, hemocyanins are not confined in blood cells, but are instead suspended directly in the hemolymph. Oxygenation causes a color change between the colorless Cu(I) deoxygenated form and the blue Cu(II) oxygenated form.

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