eF-site ID 4yzf-CDIJKL PDB Code 4yzf Chain C, D, I, J, K, L 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 C:  GLVRDIRRRYPYYLSDITDAFSPQVLAAVIFIYFAALSPA ITFGGLLGEKTRNQMGVSELLISTAVQGILFALLGAQPLL VVGFSGPLLVFEEAFFSFCETNGLEYIVGRVWIGFWLILL VVLVVAFEGSFLVRFISRYTQEIFSFLISLIFIYETFSKL IKIFQDHPLQKTYLPNTALLSLVLMAGTFFFAMMLRKFKN SSYFPGKLRRVIGDFGVPISILIMVLVDFFIQDTYTQKLS VPDGFKVVIHPLGLRSEFPIWMMFASALPALLVFILIFLE SQITTLIVSKPERKMVKGSGFHLDLLLVVGMGGVAALFGM PWLSATTVRSVTHANALTVMIQEVKEQRISGLLVAVLVGL SILMEPILSRIPLAVLFGIFLYMGVTSLSGIQLFDRILLL FKPPKYHPDVPYVKRVKTWRMHLFTGIQIICLAVLWVVKS TPASLALPFVLILTVPLRRVLLPLIFRNVELQCLD D:  GLVRDIRRRYPYYLSDITDAFSPQVLAAVIFIYFAALSPA ITFGGLLGEKTRNQMGVSELLISTAVQGILFALLGAQPLL VVGFSGPLLVFEEAFFSFCETNGLEYIVGRVWIGFWLILL VVLVVAFEGSFLVRFISRYTQEIFSFLISLIFIYETFSKL IKIFQDHPLQKTYLPNTALLSLVLMAGTFFFAMMLRKFKN SSYFPGKLRRVIGDFGVPISILIMVLVDFFIQDTYTQKLS VPDGFKVVIHPLGLRSEFPIWMMFASALPALLVFILIFLE SQITTLIVSKPERKMVKGSGFHLDLLLVVGMGGVAALFGM PWLSATTVRSVTHANALTVMIQEVKEQRISGLLVAVLVGL SILMEPILSRIPLAVLFGIFLYMGVTSLSGIQLFDRILLL FKPPKYHPDVPYVKRVKTWRMHLFTGIQIICLAVLWVVKS TPASLALPFVLILTVPLRRVLLPLIFRNVELQCLD I:  EVKLQESGPGKLQPSQTLSLTCSFSGFSLTTSGIGVGWIR QPSGKGLEWLAHIWWSASKYYNTALKSRLTISKDTSNNQV FLKIASVDTADTATYYCARAYYGNYGGYYFDYWGQGTTLT VSSAKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPV TLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPS QSITCNVAHPASSTKVDKKIEPR J:  DIVMTQSPASLAVSLGQRATISCRASQSVSTSSYSYMNWY QQKPGQPPKLLIKYASNLESGVPARFSGSGSGTDFTLNIH PLEEEDTATYYCQHSWEIPWTFGGGTKVEIKRADAAPTVS IFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQ NGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEA THKTSTSPIVKSFNRNEC K:  EVKLQESGPGKLQPSQTLSLTCSFSGFSLTTSGIGVGWIR QPSGKGLEWLAHIWWSASKYYNTALKSRLTISKDTSNNQV FLKIASVDTADTATYYCARAYYGNYGGYYFDYWGQGTTLT VSSAKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPV TLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPS QSITCNVAHPASSTKVDKKIEPR L:  DIVMTQSPASLAVSLGQRATISCRASQSVSTSSYSYMNWY QQKPGQPPKLLIKYASNLESGVPARFSGSGSGTDFTLNIH PLEEEDTATYYCQHSWEIPWTFGGGTKVEIKRADAAPTVS IFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQ NGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEA THKTSTSPIVKSFNRNEC 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 C residue 419 type sequence P description binding site for residue 4KU C 1000 source : AC3 2) chain C residue 422 type sequence T description binding site for residue 4KU C 1000 source : AC3 3) chain C residue 467 type sequence P description binding site for residue 4KU C 1000 source : AC3 4) chain C residue 532 type sequence F description binding site for residue 4KU C 1000 source : AC3 5) chain C residue 535 type sequence E description binding site for residue 4KU C 1000 source : AC3 6) chain C residue 539 type sequence K description binding site for residue 4KU C 1000 source : AC3 7) chain C residue 792 type sequence F description binding site for residue 4KU C 1000 source : AC3 8) chain C residue 851 type sequence K description binding site for residue 4KU C 1000 source : AC3 9) chain D residue 419 type sequence P description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 10) chain D residue 422 type sequence T description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 11) chain D residue 467 type sequence P description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 12) chain D residue 531 type sequence I description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 13) chain D residue 532 type sequence F description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 14) chain D residue 535 type sequence E description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 15) chain D residue 539 type sequence K description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 16) chain D residue 847 type sequence L description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 17) chain D residue 849 type sequence V description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 18) chain D residue 850 type sequence V description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 19) chain D residue 852 type sequence S description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 20) chain D residue 853 type sequence T description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 21) chain D residue 856 type sequence S description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 22) chain D residue 859 type sequence L description binding site for Di-peptide 4KU D 1000 and LYS D 851 source : AC4 23) chain D residue 419 type sequence P description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 24) chain D residue 422 type sequence T description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 25) chain D residue 467 type sequence P description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 26) chain D residue 532 type sequence F description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 27) chain D residue 535 type sequence E description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 28) chain D residue 536 type sequence T description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 29) chain D residue 537 type sequence F description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 30) chain D residue 538 type sequence S description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 31) chain D residue 540 type sequence L description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 32) chain D residue 541 type sequence I description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 33) chain D residue 542 type sequence K description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 34) chain D residue 543 type sequence I description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 35) chain D residue 789 type sequence F description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 36) chain D residue 851 type sequence K description binding site for Di-peptide 4KU D 1000 and LYS D 539 source : AC5 37) chain C residue 843 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:1885574 source Swiss-Prot : SWS_FT_FI24 38) chain D residue 843 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:1885574 source Swiss-Prot : SWS_FT_FI24 39) chain C residue 404-427 type TRANSMEM sequence QVLAAVIFIYFAALSPAITFGGLL description Helical; Name=1 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI2 40) chain D residue 404-427 type TRANSMEM sequence QVLAAVIFIYFAALSPAITFGGLL description Helical; Name=1 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI2 41) chain C residue 477-485 type TOPO_DOM sequence SFCETNGLE description Extracellular => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI3 42) chain C residue 542-570 type TOPO_DOM sequence KIFQDHPLQKTYLPNT description Extracellular => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI3 43) chain C residue 624-663 type TOPO_DOM sequence IQDTYTQKLSVPDGFKVVIHPLGLRSEFPIWM description Extracellular => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI3 44) chain D residue 428-435 type TOPO_DOM sequence GEKTRNQM description Extracellular => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI3 45) chain D residue 477-485 type TOPO_DOM sequence SFCETNGLE description Extracellular => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI3 46) chain D residue 542-570 type TOPO_DOM sequence KIFQDHPLQKTYLPNT description Extracellular => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI3 47) chain D residue 624-663 type TOPO_DOM sequence IQDTYTQKLSVPDGFKVVIHPLGLRSEFPIWM description Extracellular => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI3 48) chain C residue 428-435 type TOPO_DOM sequence GEKTRNQM description Extracellular => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI3 49) chain C residue 436-456 type TRANSMEM sequence GVSELLISTAVQGILFALLGA description Helical; Name=2 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI4 50) chain D residue 436-456 type TRANSMEM sequence GVSELLISTAVQGILFALLGA description Helical; Name=2 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI4 51) chain C residue 460-476 type TRANSMEM sequence LVVGFSGPLLVFEEAFF description Discontinuously helical; Name=3 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI5 52) chain D residue 460-476 type TRANSMEM sequence LVVGFSGPLLVFEEAFF description Discontinuously helical; Name=3 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI5 53) chain C residue 486-506 type TRANSMEM sequence YIVGRVWIGFWLILLVVLVVA description Helical; Name=4 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI6 54) chain D residue 486-506 type TRANSMEM sequence YIVGRVWIGFWLILLVVLVVA description Helical; Name=4 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI6 55) chain C residue 519-541 type TRANSMEM sequence YTQEIFSFLISLIFIYETFSKLI description Helical; Name=5 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI7 56) chain D residue 519-541 type TRANSMEM sequence YTQEIFSFLISLIFIYETFSKLI description Helical; Name=5 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI7 57) chain C residue 571-591 type TRANSMEM sequence ALLSLVLMAGTFFFAMMLRKF description Helical; Name=6 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI8 58) chain D residue 571-591 type TRANSMEM sequence ALLSLVLMAGTFFFAMMLRKF description Helical; Name=6 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI8 59) chain C residue 603-623 type TRANSMEM sequence RVIGDFGVPISILIMVLVDFF description Helical; Name=7 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI9 60) chain D residue 603-623 type TRANSMEM sequence RVIGDFGVPISILIMVLVDFF description Helical; Name=7 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI9 61) chain C residue 457-459 type TOPO_DOM sequence QPL description Cytoplasmic => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI1 62) chain C residue 507-518 type TOPO_DOM sequence FEGSFLVRFISR description Cytoplasmic => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI1 63) chain C residue 592-602 type TOPO_DOM sequence KNSSYFPGKLR description Cytoplasmic => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI1 64) chain C residue 685-700 type TOPO_DOM sequence TTLIVSKPERKMVKGS description Cytoplasmic => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI1 65) chain C residue 738-760 type TOPO_DOM sequence LTVMIQEVKEQR description Cytoplasmic => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI1 66) chain C residue 801-838 type TOPO_DOM sequence SGIQLFDRILLLFKPPKYHPDVPYVKRVKTWRMHLFTG description Cytoplasmic => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI1 67) chain D residue 457-459 type TOPO_DOM sequence QPL description Cytoplasmic => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI1 68) chain D residue 507-518 type TOPO_DOM sequence FEGSFLVRFISR description Cytoplasmic => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI1 69) chain D residue 592-602 type TOPO_DOM sequence KNSSYFPGKLR description Cytoplasmic => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI1 70) chain D residue 685-700 type TOPO_DOM sequence TTLIVSKPERKMVKGS description Cytoplasmic => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI1 71) chain D residue 738-760 type TOPO_DOM sequence LTVMIQEVKEQR description Cytoplasmic => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI1 72) chain D residue 801-838 type TOPO_DOM sequence SGIQLFDRILLLFKPPKYHPDVPYVKRVKTWRMHLFTG description Cytoplasmic => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI1 73) chain C residue 664-684 type TRANSMEM sequence MFASALPALLVFILIFLESQI description Helical; Name=8 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI10 74) chain D residue 664-684 type TRANSMEM sequence MFASALPALLVFILIFLESQI description Helical; Name=8 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI10 75) chain C residue 701-719 type TRANSMEM sequence GFHLDLLLVVGMGGVAALF description Helical; Name=9 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI11 76) chain D residue 701-719 type TRANSMEM sequence GFHLDLLLVVGMGGVAALF description Helical; Name=9 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI11 77) chain C residue 720-737 type TRANSMEM sequence GMPWLSATTVRSVTHANA description Discontinuously helical; Name=10 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI12 78) chain D residue 720-737 type TRANSMEM sequence GMPWLSATTVRSVTHANA description Discontinuously helical; Name=10 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI12 79) chain C residue 761-781 type TRANSMEM sequence ISGLLVAVLVGLSILMEPILS description Helical; Name=11 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI13 80) chain D residue 761-781 type TRANSMEM sequence ISGLLVAVLVGLSILMEPILS description Helical; Name=11 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI13 81) chain C residue 782-800 type TRANSMEM sequence RIPLAVLFGIFLYMGVTSL description Helical; Name=12 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI14 82) chain D residue 782-800 type TRANSMEM sequence RIPLAVLFGIFLYMGVTSL description Helical; Name=12 => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI14 83) chain C residue 590 type SITE sequence K description Important for anion transport source Swiss-Prot : SWS_FT_FI16 84) chain D residue 590 type SITE sequence K description Important for anion transport source Swiss-Prot : SWS_FT_FI16 85) chain C residue 681 type SITE sequence E description Important for anion-proton cotransport source Swiss-Prot : SWS_FT_FI17 86) chain D residue 681 type SITE sequence E description Important for anion-proton cotransport source Swiss-Prot : SWS_FT_FI17 87) chain C residue 839-869 type INTRAMEM sequence IQIICLAVLWVVKSTPASLALPFVLILTVPL description Discontinuously helical => ECO:0000269|PubMed:26542571 source Swiss-Prot : SWS_FT_FI15 88) 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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