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1HCY

CRYSTAL STRUCTURE OF HEXAMERIC HAEMOCYANIN FROM PANULIRUS INTERRUPTUS REFINED AT 3.2 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0005344molecular_functionoxygen carrier activity
A0005576cellular_componentextracellular region
A0015671biological_processoxygen transport
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
B0005344molecular_functionoxygen carrier activity
B0005576cellular_componentextracellular region
B0015671biological_processoxygen transport
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
C0005344molecular_functionoxygen carrier activity
C0005576cellular_componentextracellular region
C0015671biological_processoxygen transport
C0016491molecular_functionoxidoreductase activity
C0046872molecular_functionmetal ion binding
D0005344molecular_functionoxygen carrier activity
D0005576cellular_componentextracellular region
D0015671biological_processoxygen transport
D0016491molecular_functionoxidoreductase activity
D0046872molecular_functionmetal ion binding
E0005344molecular_functionoxygen carrier activity
E0005576cellular_componentextracellular region
E0015671biological_processoxygen transport
E0016491molecular_functionoxidoreductase activity
E0046872molecular_functionmetal ion binding
F0005344molecular_functionoxygen carrier activity
F0005576cellular_componentextracellular region
F0015671biological_processoxygen transport
F0016491molecular_functionoxidoreductase activity
F0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00209
Number of Residues20
DetailsHEMOCYANIN_1 Arthropod hemocyanins / insect LSPs signature 1. YFgEDIgmNihhvtwHmdfP
ChainResidueDetails
ATYR183-PRO202

site_idPS00210
Number of Residues9
DetailsHEMOCYANIN_2 Arthropod hemocyanins / insect LSPs signature 2. TatRDPsFF
ChainResidueDetails
ATHR373-PHE381

site_idPS00498
Number of Residues12
DetailsTYROSINASE_2 Tyrosinase and hemocyanins CuB-binding region signature. DPsFFrlHkymD
ChainResidueDetails
AASP377-ASP388

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues36
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"2585484","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HC1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HCY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"2585484","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HCY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1bt1
ChainResidueDetails
ATYR340

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1bt1
ChainResidueDetails
BTYR340

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1bt1
ChainResidueDetails
CTYR340

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1bt1
ChainResidueDetails
DTYR340

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1bt1
ChainResidueDetails
ETYR340

site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1bt1
ChainResidueDetails
FTYR340

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PDB entries from 2025-10-08

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