Structure of PDB 1oxy Chain A

Receptor sequence
>1oxyA (length=573) Species: 6850 (Limulus polyphemus) [Search protein sequence]
TLHDKQIRICHLFEQLSRLKNVGKLQPGAIFSCFHPDHLEEARHLYEVFW
EAGDFNDFIEIAKEARTFVNEGLFAFAAEVAVLHRDDCKGLYVPPVQEIF
PDKFIPSAAINEAFKKGNILDPEYRLAYYREDVGINAHHWHWHLVYPSTW
NPKYFGKKKDRKGELFYYMHQQMCARYDCERLSNGMHRMLPFNNFDEPLA
GYAPHLTHVASGKYYSPRPDGLKLRDLGDIEISEMVRMRERILDSIHLGY
VISEDGSHKTLDELHGTDILGALVESSYESVNHEYYGNLHNWGHVTMARI
HDPDGRFHEEPGVMSDTSTSLRDPIFYNWHRFIDNIFHEYKNTLKPYDHD
VLNFPDIQVQDVTLHARVDNVVHTFMREQELELKHGSIKAKYYHLDHEPF
SYAVNVQNNSASDKHATVRIFLAPKYDELGNEIKADELRRTAIELDKFKT
DLHPGKNTVVRHSLDSSVTLSHQPTFEDLLSEYCSCGWPSHLLVPKGNVA
GMEYHLFVMLTDWDKDKVDVACVDAVSYCGARDHKYPDKKPMGFPFDRPI
HTEHISDFLTNNMFIKDIKIKFH
3D structure
PDB1oxy Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences.
ChainA
Resolution2.4 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CU A H324 H328 H364 H290 H294 H330
BS02 CU A H173 H177 H204 H139 H143 H170
BS03 OXY A H173 H177 H204 H324 H328 H139 H143 H170 H290 H294
Gene Ontology
Molecular Function
GO:0005344 oxygen carrier activity
GO:0005507 copper ion binding
GO:0016491 oxidoreductase activity
GO:0031404 chloride ion binding
GO:0046872 metal ion binding
Biological Process
GO:0015671 oxygen transport
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1oxy, PDBe:1oxy, PDBj:1oxy
PDBsum1oxy
PubMed7984626
UniProtP04253|HCY2_LIMPO Hemocyanin II

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