Structure of PDB 1ll1 Chain A

Receptor sequence
>1ll1A (length=590) Species: 6850 (Limulus polyphemus) [Search protein sequence]
TLHDKQIRVCHLFEQLSSATVIRLKNVGKLQPGAIFSCFHPDHLEEARHL
YEVFWEAGDFNDFIEIAKEARTFVNEGLFAFAAEVAVLHRDDCKGLYVPP
VQEIFPDKFIPSAAINEAFKKILVDVGNILDPEYRLAYYREDVGINAHHW
HWHLVYPSTWNPKYFGKKKDRKGELFYYMHQQMCARYDCERLSNGMHRML
PFNNFDEPLAGYAPHLTHVASGKYYSPRPDGLKLRDLGDIEISEMVRMRE
RILDSIHLGYVISEDGSHKTLDELHGTDILGALVESSYESVNHEYYGNLH
NWGHVTMARIHDPDGRFHEEPGVMSDTSTSLRDPIFYNWHRFIDNIFHEY
KNTLKPYDHDVLNFPDIQVQDVTLHARVDNVVHTFMREQELELKHGINPG
NARSIKARYYHLDHEPFSYAVNVQNNSASDKHATVRIFLAPKYDELGNEI
KADELRRTAIELDKFKTDLHPGKNTVVRHSLDSSVTLSHQPTFEDLLSEY
CSCGWPSHLLVPKGNIKGMEYHLFVMLTDWDKDKVVACVDAVSYCGARDH
KYPDKKPMGFPFDRPIHTEHISDFLTNNMFIKDIKIKFHE
3D structure
PDB1ll1 Crystallographic Studies of Hydroxo, Nitrosyl, Azido and Fluro met Form Hemocyanin Subunit II from Limulus
ChainA
Resolution2.55 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 H300 H304 H340
BS02 CU A H173 H177 H204 H149 H153 H180
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:1ll1, PDBe:1ll1, PDBj:1ll1
PDBsum1ll1
PubMed
UniProtP04253|HCY2_LIMPO Hemocyanin II

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