eF-site ID 1hcy-ABCDEF PDB Code 1hcy Chain A, B, C, D, E, F Title CRYSTAL STRUCTURE OF HEXAMERIC HAEMOCYANIN FROM PANULIRUS INTERRUPTUS REFINED AT 3.2 ANGSTROMS RESOLUTION Classification OXYGEN TRANSPORT Compound ARTHROPODAN HEMOCYANIN Source ORGANISM_COMMON: California spiny lobster; ORGANISM_SCIENTIFIC: Panulirus interruptus; Sequence A:  DALGTGNAQKQQDINHLLDKIYEPTKYPDLKDIAENFNPL GDTSIYNDHGAAVETLMKELNDHRLLEQRHWYSLFNTRQR KEALMLFAVLNQCKEWYCFRSNAAYFRERMNEGEFVYALY VSVIHSKLGDGIVLPPLYQITPHMFTNSEVIDKAYSAKMT QKPGTFNVSFTGTKKNREQRVAYFGEDIGMNIHHVTWHMD FPFWWEDSYGYHLDRKGELFFWVHHQLTARFDFERLSNWL DPVDELHWDRIIREGFAPLTSYKYGGEFPVRPDNIHFEDV DGVAHVHDLEITESRIHEAIDHGYITDSDGHTIDIRQPKG IELLGDIIESSKYSSNVQYYGSLHNTAHVMLGRQGDPHGK FNLPPGVMEHFETATRDPSFFRLHKYMDNIFKKHTDSFPP YTHDNLEFSGMVVNGVAIDGELITFFDEFQYSLINAVDSG ENIEDVEINARVHRLNHNEFTYKITMSNNNDGERLATFRI FLCPIEDNNGITLTLDEARWFCIELDKFFQKVPSGPETIE RSSKDSSVTVPDMPSFQSLKEQADNAVNGGHDLDLSAYER SCGIPDRMLLPKSKPEGMEFNLYVAVTDGDKDTEGHHAQC GVHGEAYPDNRPLGYPLERRIPDERVIDGVSNIKHVVVKI VHHL B:  DALGTGNAQKQQDINHLLDKIYEPTKYPDLKDIAENFNPL GDTSIYNDHGAAVETLMKELNDHRLLEQRHWYSLFNTRQR KEALMLFAVLNQCKEWYCFRSNAAYFRERMNEGEFVYALY VSVIHSKLGDGIVLPPLYQITPHMFTNSEVIDKAYSAKMT QKPGTFNVSFTGTKKNREQRVAYFGEDIGMNIHHVTWHMD FPFWWEDSYGYHLDRKGELFFWVHHQLTARFDFERLSNWL DPVDELHWDRIIREGFAPLTSYKYGGEFPVRPDNIHFEDV DGVAHVHDLEITESRIHEAIDHGYITDSDGHTIDIRQPKG IELLGDIIESSKYSSNVQYYGSLHNTAHVMLGRQGDPHGK FNLPPGVMEHFETATRDPSFFRLHKYMDNIFKKHTDSFPP YTHDNLEFSGMVVNGVAIDGELITFFDEFQYSLINAVDSG ENIEDVEINARVHRLNHNEFTYKITMSNNNDGERLATFRI FLCPIEDNNGITLTLDEARWFCIELDKFFQKVPSGPETIE RSSKDSSVTVPDMPSFQSLKEQADNAVNGGHDLDLSAYER SCGIPDRMLLPKSKPEGMEFNLYVAVTDGDKDTEGHHAQC GVHGEAYPDNRPLGYPLERRIPDERVIDGVSNIKHVVVKI VHHL C:  DALGTGNAQKQQDINHLLDKIYEPTKYPDLKDIAENFNPL GDTSIYNDHGAAVETLMKELNDHRLLEQRHWYSLFNTRQR KEALMLFAVLNQCKEWYCFRSNAAYFRERMNEGEFVYALY VSVIHSKLGDGIVLPPLYQITPHMFTNSEVIDKAYSAKMT QKPGTFNVSFTGTKKNREQRVAYFGEDIGMNIHHVTWHMD FPFWWEDSYGYHLDRKGELFFWVHHQLTARFDFERLSNWL DPVDELHWDRIIREGFAPLTSYKYGGEFPVRPDNIHFEDV DGVAHVHDLEITESRIHEAIDHGYITDSDGHTIDIRQPKG IELLGDIIESSKYSSNVQYYGSLHNTAHVMLGRQGDPHGK FNLPPGVMEHFETATRDPSFFRLHKYMDNIFKKHTDSFPP YTHDNLEFSGMVVNGVAIDGELITFFDEFQYSLINAVDSG ENIEDVEINARVHRLNHNEFTYKITMSNNNDGERLATFRI FLCPIEDNNGITLTLDEARWFCIELDKFFQKVPSGPETIE RSSKDSSVTVPDMPSFQSLKEQADNAVNGGHDLDLSAYER SCGIPDRMLLPKSKPEGMEFNLYVAVTDGDKDTEGHHAQC GVHGEAYPDNRPLGYPLERRIPDERVIDGVSNIKHVVVKI VHHL D:  DALGTGNAQKQQDINHLLDKIYEPTKYPDLKDIAENFNPL GDTSIYNDHGAAVETLMKELNDHRLLEQRHWYSLFNTRQR KEALMLFAVLNQCKEWYCFRSNAAYFRERMNEGEFVYALY VSVIHSKLGDGIVLPPLYQITPHMFTNSEVIDKAYSAKMT QKPGTFNVSFTGTKKNREQRVAYFGEDIGMNIHHVTWHMD FPFWWEDSYGYHLDRKGELFFWVHHQLTARFDFERLSNWL DPVDELHWDRIIREGFAPLTSYKYGGEFPVRPDNIHFEDV DGVAHVHDLEITESRIHEAIDHGYITDSDGHTIDIRQPKG IELLGDIIESSKYSSNVQYYGSLHNTAHVMLGRQGDPHGK FNLPPGVMEHFETATRDPSFFRLHKYMDNIFKKHTDSFPP YTHDNLEFSGMVVNGVAIDGELITFFDEFQYSLINAVDSG ENIEDVEINARVHRLNHNEFTYKITMSNNNDGERLATFRI FLCPIEDNNGITLTLDEARWFCIELDKFFQKVPSGPETIE RSSKDSSVTVPDMPSFQSLKEQADNAVNGGHDLDLSAYER SCGIPDRMLLPKSKPEGMEFNLYVAVTDGDKDTEGHHAQC GVHGEAYPDNRPLGYPLERRIPDERVIDGVSNIKHVVVKI VHHL E:  DALGTGNAQKQQDINHLLDKIYEPTKYPDLKDIAENFNPL GDTSIYNDHGAAVETLMKELNDHRLLEQRHWYSLFNTRQR KEALMLFAVLNQCKEWYCFRSNAAYFRERMNEGEFVYALY VSVIHSKLGDGIVLPPLYQITPHMFTNSEVIDKAYSAKMT QKPGTFNVSFTGTKKNREQRVAYFGEDIGMNIHHVTWHMD FPFWWEDSYGYHLDRKGELFFWVHHQLTARFDFERLSNWL DPVDELHWDRIIREGFAPLTSYKYGGEFPVRPDNIHFEDV DGVAHVHDLEITESRIHEAIDHGYITDSDGHTIDIRQPKG IELLGDIIESSKYSSNVQYYGSLHNTAHVMLGRQGDPHGK FNLPPGVMEHFETATRDPSFFRLHKYMDNIFKKHTDSFPP YTHDNLEFSGMVVNGVAIDGELITFFDEFQYSLINAVDSG ENIEDVEINARVHRLNHNEFTYKITMSNNNDGERLATFRI FLCPIEDNNGITLTLDEARWFCIELDKFFQKVPSGPETIE RSSKDSSVTVPDMPSFQSLKEQADNAVNGGHDLDLSAYER SCGIPDRMLLPKSKPEGMEFNLYVAVTDGDKDTEGHHAQC GVHGEAYPDNRPLGYPLERRIPDERVIDGVSNIKHVVVKI VHHL F:  DALGTGNAQKQQDINHLLDKIYEPTKYPDLKDIAENFNPL GDTSIYNDHGAAVETLMKELNDHRLLEQRHWYSLFNTRQR KEALMLFAVLNQCKEWYCFRSNAAYFRERMNEGEFVYALY VSVIHSKLGDGIVLPPLYQITPHMFTNSEVIDKAYSAKMT QKPGTFNVSFTGTKKNREQRVAYFGEDIGMNIHHVTWHMD FPFWWEDSYGYHLDRKGELFFWVHHQLTARFDFERLSNWL DPVDELHWDRIIREGFAPLTSYKYGGEFPVRPDNIHFEDV DGVAHVHDLEITESRIHEAIDHGYITDSDGHTIDIRQPKG IELLGDIIESSKYSSNVQYYGSLHNTAHVMLGRQGDPHGK FNLPPGVMEHFETATRDPSFFRLHKYMDNIFKKHTDSFPP YTHDNLEFSGMVVNGVAIDGELITFFDEFQYSLINAVDSG ENIEDVEINARVHRLNHNEFTYKITMSNNNDGERLATFRI FLCPIEDNNGITLTLDEARWFCIELDKFFQKVPSGPETIE RSSKDSSVTVPDMPSFQSLKEQADNAVNGGHDLDLSAYER SCGIPDRMLLPKSKPEGMEFNLYVAVTDGDKDTEGHHAQC GVHGEAYPDNRPLGYPLERRIPDERVIDGVSNIKHVVVKI VHHL Description (1)  ARTHROPODAN HEMOCYANIN (DEOXYGENATED) REFINED USING CONSTRAINED 32 POINT GROUP SYMMETRY Functional site 1) chain A residue 194 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 2) chain B residue 344 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 3) chain B residue 348 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 4) chain B residue 384 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 5) chain C residue 194 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 6) chain C residue 198 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 7) chain C residue 224 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 8) chain C residue 344 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 9) chain C residue 348 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 10) chain C residue 384 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 11) chain D residue 194 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 12) chain A residue 198 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 13) chain D residue 198 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 14) chain D residue 224 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 15) chain D residue 344 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 16) chain D residue 348 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 17) chain D residue 384 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 18) chain E residue 194 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 19) chain E residue 198 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 20) chain E residue 224 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 21) chain E residue 344 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 22) chain E residue 348 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 23) chain A residue 224 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 24) chain E residue 384 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 25) chain F residue 194 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 26) chain F residue 198 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 27) chain F residue 224 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 28) chain F residue 344 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 29) chain F residue 348 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 30) chain F residue 384 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 31) chain A residue 344 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 32) chain A residue 348 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 33) chain A residue 384 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 34) chain B residue 194 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 35) chain B residue 198 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 36) chain B residue 224 type BINDING sequence H description BINDING => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI1 37) chain A residue 167 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI2 38) chain B residue 167 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI2 39) chain C residue 167 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI2 40) chain D residue 167 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI2 41) chain E residue 167 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI2 42) chain F residue 167 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:2585484, ECO:0007744|PDB:1HCY source Swiss-Prot : SWS_FT_FI2 43) chain A residue 183-202 type prosite sequence YFGEDIGMNIHHVTWHMDFP description HEMOCYANIN_1 Arthropod hemocyanins / insect LSPs signature 1. YFgEDIgmNihhvtwHmdfP source prosite : PS00209 44) chain A residue 373-381 type prosite sequence TATRDPSFF description HEMOCYANIN_2 Arthropod hemocyanins / insect LSPs signature 2. TatRDPsFF source prosite : PS00210 45) chain A residue 377-388 type prosite sequence DPSFFRLHKYMD description TYROSINASE_2 Tyrosinase and hemocyanins CuB-binding region signature. DPsFFrlHkymD source prosite : PS00498

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