eF-site ID 4yzf-D PDB Code 4yzf Chain D click to enlarge Title Crystal structure of the anion exchanger domain of human erythrocyte Band 3 Classification IMMUNE SYSTEM Compound Band 3 anion transport protein Source ORGANISM_COMMON: Human; ORGANISM_SCIENTIFIC: Homo sapiens; Sequence D:  GLVRDIRRRYPYYLSDITDAFSPQVLAAVIFIYFAALSPA ITFGGLLGEKTRNQMGVSELLISTAVQGILFALLGAQPLL VVGFSGPLLVFEEAFFSFCETNGLEYIVGRVWIGFWLILL VVLVVAFEGSFLVRFISRYTQEIFSFLISLIFIYETFSKL IKIFQDHPLQKTYLPNTALLSLVLMAGTFFFAMMLRKFKN SSYFPGKLRRVIGDFGVPISILIMVLVDFFIQDTYTQKLS VPDGFKVVIHPLGLRSEFPIWMMFASALPALLVFILIFLE SQITTLIVSKPERKMVKGSGFHLDLLLVVGMGGVAALFGM PWLSATTVRSVTHANALTVMIQEVKEQRISGLLVAVLVGL SILMEPILSRIPLAVLFGIFLYMGVTSLSGIQLFDRILLL FKPPKYHPDVPYVKRVKTWRMHLFTGIQIICLAVLWVVKS TPASLALPFVLILTVPLRRVLLPLIFRNVELQCLD Description (1)  Outward facing structure of human anion exchanger 1 (Band 3) in co-crystallised with FAB antibody fragments. , FAB fragment of Immunoglobulin (IgG) molecule Functional site 1) chain D residue 419 type sequence P description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 2) chain D residue 422 type sequence T description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 3) chain D residue 467 type sequence P description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 4) chain D residue 531 type sequence I description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 5) chain D residue 532 type sequence F description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 6) chain D residue 535 type sequence E description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 7) chain D residue 539 type sequence K description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 8) chain D residue 847 type sequence L description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 9) chain D residue 849 type sequence V description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 10) chain D residue 850 type sequence V description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 11) chain D residue 852 type sequence S description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 12) chain D residue 853 type sequence T description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 13) chain D residue 856 type sequence S description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 14) chain D residue 859 type sequence L description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 15) chain D residue 419 type sequence P description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 16) chain D residue 422 type sequence T description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 17) chain D residue 467 type sequence P description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 18) chain D residue 532 type sequence F description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 19) chain D residue 535 type sequence E description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 20) chain D residue 536 type sequence T description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 21) chain D residue 537 type sequence F description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 22) chain D residue 538 type sequence S description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 23) chain D residue 540 type sequence L description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 24) chain D residue 541 type sequence I description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 25) chain D residue 542 type sequence K description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 26) chain D residue 543 type sequence I description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 27) chain D residue 789 type sequence F description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 28) chain D residue 851 type sequence K description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 29) chain D residue 843 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:1885574 source Swiss-Prot : SWS_FT_FI24 30) chain D residue 404-427 type TRANSMEM sequence QVLAAVIFIYFAALSPAITFGGLL description Helical; Name=1 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI2 31) chain D residue 428-435 type TOPO_DOM sequence GEKTRNQM description Extracellular => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI3 32) chain D residue 477-485 type TOPO_DOM sequence SFCETNGLE description Extracellular => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI3 33) chain D residue 542-570 type TOPO_DOM sequence KIFQDHPLQKTYLPNT description Extracellular => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI3 34) chain D residue 624-663 type TOPO_DOM sequence IQDTYTQKLSVPDGFKVVIHPLGLRSEFPIWM description Extracellular => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI3 35) chain D residue 436-456 type TRANSMEM sequence GVSELLISTAVQGILFALLGA description Helical; Name=2 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI4 36) chain D residue 460-476 type TRANSMEM sequence LVVGFSGPLLVFEEAFF description Discontinuously helical; Name=3 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI5 37) chain D residue 486-506 type TRANSMEM sequence YIVGRVWIGFWLILLVVLVVA description Helical; Name=4 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI6 38) chain D residue 519-541 type TRANSMEM sequence YTQEIFSFLISLIFIYETFSKLI description Helical; Name=5 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI7 39) chain D residue 571-591 type TRANSMEM sequence ALLSLVLMAGTFFFAMMLRKF description Helical; Name=6 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI8 40) chain D residue 603-623 type TRANSMEM sequence RVIGDFGVPISILIMVLVDFF description Helical; Name=7 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI9 41) chain D residue 457-459 type TOPO_DOM sequence QPL description Cytoplasmic => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI1 42) chain D residue 507-518 type TOPO_DOM sequence FEGSFLVRFISR description Cytoplasmic => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI1 43) chain D residue 592-602 type TOPO_DOM sequence KNSSYFPGKLR description Cytoplasmic => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI1 44) chain D residue 685-700 type TOPO_DOM sequence TTLIVSKPERKMVKGS description Cytoplasmic => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI1 45) chain D residue 738-760 type TOPO_DOM sequence LTVMIQEVKEQR description Cytoplasmic => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI1 46) chain D residue 801-838 type TOPO_DOM sequence SGIQLFDRILLLFKPPKYHPDVPYVKRVKTWRMHLFTG description Cytoplasmic => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI1 47) chain D residue 664-684 type TRANSMEM sequence MFASALPALLVFILIFLESQI description Helical; Name=8 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI10 48) chain D residue 701-719 type TRANSMEM sequence GFHLDLLLVVGMGGVAALF description Helical; Name=9 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI11 49) chain D residue 720-737 type TRANSMEM sequence GMPWLSATTVRSVTHANA description Discontinuously helical; Name=10 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI12 50) chain D residue 761-781 type TRANSMEM sequence ISGLLVAVLVGLSILMEPILS description Helical; Name=11 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI13 51) chain D residue 782-800 type TRANSMEM sequence RIPLAVLFGIFLYMGVTSL description Helical; Name=12 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI14 52) chain D residue 590 type SITE sequence K description Important for anion transport source Swiss-Prot : SWS_FT_FI16 53) chain D residue 681 type SITE sequence E description Important for anion-proton cotransport source Swiss-Prot : SWS_FT_FI17 54) chain D residue 839-869 type INTRAMEM sequence IQIICLAVLWVVKSTPASLALPFVLILTVPL description Discontinuously helical => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI15

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