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1HC1

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

Replaces:  1HC2Replaces:  1HC3Replaces:  1HC4Replaces:  1HC5Replaces:  1HC6
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 PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 665
ChainResidue
AHIS194
AHIS198
AHIS224
ACU666

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 666
ChainResidue
AHIS344
AHIS348
AHIS384
ACU665

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU B 665
ChainResidue
BHIS198
BHIS224
BPHE371
BHIS194

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU B 666
ChainResidue
BHIS344
BHIS348
BHIS384

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU C 665
ChainResidue
CHIS194
CHIS198
CHIS224
CCU666

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU C 666
ChainResidue
CHIS344
CHIS348
CHIS384
CCU665

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU D 665
ChainResidue
DHIS194
DHIS198
DHIS224
DCU666

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU D 666
ChainResidue
DHIS344
DHIS348
DHIS384
DCU665

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU E 665
ChainResidue
EHIS194
EHIS198
EHIS224
ECU666

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU E 666
ChainResidue
EHIS344
EHIS348
EHIS384
ECU665

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU F 665
ChainResidue
FHIS194
FHIS198
FHIS224
FCU666

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU F 666
ChainResidue
FHIS344
FHIS348
FHIS384
FCU665

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: BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY
ChainResidueDetails
AHIS194
BHIS344
BHIS348
BHIS384
CHIS194
CHIS198
CHIS224
CHIS344
CHIS348
CHIS384
DHIS194
AHIS198
DHIS198
DHIS224
DHIS344
DHIS348
DHIS384
EHIS194
EHIS198
EHIS224
EHIS344
EHIS348
AHIS224
EHIS384
FHIS194
FHIS198
FHIS224
FHIS344
FHIS348
FHIS384
AHIS344
AHIS348
AHIS384
BHIS194
BHIS198
BHIS224

site_idSWS_FT_FI2
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HCY
ChainResidueDetails
AASN167
BASN167
CASN167
DASN167
EASN167
FASN167

220113

PDB entries from 2024-05-22

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