hemoglobin complex / oxygen carrier activity / oxygen binding / response to hypoxia / iron ion binding / heme binding / extracellular region / metal ion binding Similarity search - Function
Lipocalin - #620 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1520 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1530 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1540 / Annelid erythrocruorin linker subunit, C-terminal / Erythrocruorin linker subunit, C-terminal superfamily / Extracellular hemoglobin linker subunit, heterodimerisation domain / Annelid erythrocruorin linker subunit C-terminus / Globin, extracellular / Erythrocruorin ...Lipocalin - #620 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1520 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1530 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1540 / Annelid erythrocruorin linker subunit, C-terminal / Erythrocruorin linker subunit, C-terminal superfamily / Extracellular hemoglobin linker subunit, heterodimerisation domain / Annelid erythrocruorin linker subunit C-terminus / Globin, extracellular / Erythrocruorin / : / Low-density lipoprotein receptor domain class A / Myoglobin-like, M family globin domain / Low-density lipoprotein (LDL) receptor class A, conserved site / LDL-receptor class A (LDLRA) domain signature. / LDL-receptor class A (LDLRA) domain profile. / Low-density lipoprotein receptor domain class A / Low-density lipoprotein (LDL) receptor class A repeat / LDL receptor-like superfamily / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Globin/Protoglobin / Globins / Globin domain profile. / Globin-like / Lipocalin / Globin / Globin / Helix non-globular / Globin-like superfamily / Special / Beta Barrel / Orthogonal Bundle / Mainly Beta / Mainly Alpha Similarity search - Domain/homology
SEQUENCE Authors state that the conflicts at residue 78 for chains A,E,I and residue 66 for chains ...SEQUENCE Authors state that the conflicts at residue 78 for chains A,E,I and residue 66 for chains B,F,J are possibly due to an error with the sequencing, however they can not distinguish it at the current resolution.
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