Structure of PDB 1lla Chain A

Receptor sequence
>1llaA (length=600) Species: 6850 (Limulus polyphemus) [Search protein sequence]
LHDKQIRICHLFEQLSSATHSDRLKNVGKLQPGAIFSCFHPDHLEEARHL
YEVFWEAGDFNDFIEIAKEARTFVNEGLFAFAAEVAVLHRDDCKGLYVPP
VQEIFPDKFIPSAAINEAFKKESPILVDVTGNILDPEYRLAYYREDVGIN
AHHWHWHLVYPSTWNPKYFGKKKDRKGELFYYMHQQMCARYDCERLSNGM
HRMLPFNNFDEPLAGYAPHLTHVASGKYYSPRPDGLKLRDLGDIEISEMV
RMRERILDSIHLGYVISEDGSHKTLDELHGTDILGALVESSYESVNHEYY
GNLHNWGHVTMARIHDPDGRFHEEPGVMSDTSTSLRDPIFYNWHRFIDNI
FHEYKNTLKPYDHDVLNFPDIQVQDVTLHARVDNVVHTFMREQELELKHG
INPGNARSIKARYYHLDHEPFSYAVNVQNNSASDKHATVRIFLAPKYDEL
GNEIKADELRRTAIELDKFKTDLHPGKNTVVRHSLDSSVTLSHQPTFEDL
LHGVGLSEYCSCGWPSHLLVPKGNIKGMEYHLFVMLTDWDKDKVSVACVD
AVSYCGARDHKYPDKKPMGFPFDRPIHTEHISDFLTNNMFIKDIKIKFHE
3D structure
PDB1lla Crystal structure of deoxygenated Limulus polyphemus subunit II hemocyanin at 2.18 A resolution: clues for a mechanism for allosteric regulation.
ChainA
Resolution2.18 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 H173 H177 H204 H153 H157 H184
BS02 CU A H324 H328 H364 H304 H308 H344
BS03 CL A S47 R333 S37 R313
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:1lla, PDBe:1lla, PDBj:1lla
PDBsum1lla
PubMed8518732
UniProtP04253|HCY2_LIMPO Hemocyanin II

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