eF-site ID 4yzf-C
PDB Code 4yzf
Chain C

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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
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 C
residue 843
type LIPID
sequence C
description S-palmitoyl cysteine => ECO:0000269|PubMed:1885574
source Swiss-Prot : SWS_FT_FI24

10) chain C
residue 404-427
type TRANSMEM
sequence QVLAAVIFIYFAALSPAITFGGLL
description Helical; Name=1 => ECO:0000269|PubMed:26542571
source Swiss-Prot : SWS_FT_FI2

11) chain C
residue 477-485
type TOPO_DOM
sequence SFCETNGLE
description Extracellular => ECO:0000269|PubMed:26542571
source Swiss-Prot : SWS_FT_FI3

12) chain C
residue 542-570
type TOPO_DOM
sequence KIFQDHPLQKTYLPNT
description Extracellular => ECO:0000269|PubMed:26542571
source Swiss-Prot : SWS_FT_FI3

13) chain C
residue 624-663
type TOPO_DOM
sequence IQDTYTQKLSVPDGFKVVIHPLGLRSEFPIWM
description Extracellular => ECO:0000269|PubMed:26542571
source Swiss-Prot : SWS_FT_FI3

14) chain C
residue 428-435
type TOPO_DOM
sequence GEKTRNQM
description Extracellular => ECO:0000269|PubMed:26542571
source Swiss-Prot : SWS_FT_FI3

15) chain C
residue 436-456
type TRANSMEM
sequence GVSELLISTAVQGILFALLGA
description Helical; Name=2 => ECO:0000269|PubMed:26542571
source Swiss-Prot : SWS_FT_FI4

16) chain C
residue 460-476
type TRANSMEM
sequence LVVGFSGPLLVFEEAFF
description Discontinuously helical; Name=3 => ECO:0000269|PubMed:26542571
source Swiss-Prot : SWS_FT_FI5

17) chain C
residue 486-506
type TRANSMEM
sequence YIVGRVWIGFWLILLVVLVVA
description Helical; Name=4 => ECO:0000269|PubMed:26542571
source Swiss-Prot : SWS_FT_FI6

18) chain C
residue 519-541
type TRANSMEM
sequence YTQEIFSFLISLIFIYETFSKLI
description Helical; Name=5 => ECO:0000269|PubMed:26542571
source Swiss-Prot : SWS_FT_FI7

19) chain C
residue 571-591
type TRANSMEM
sequence ALLSLVLMAGTFFFAMMLRKF
description Helical; Name=6 => ECO:0000269|PubMed:26542571
source Swiss-Prot : SWS_FT_FI8

20) chain C
residue 603-623
type TRANSMEM
sequence RVIGDFGVPISILIMVLVDFF
description Helical; Name=7 => ECO:0000269|PubMed:26542571
source Swiss-Prot : SWS_FT_FI9

21) chain C
residue 457-459
type TOPO_DOM
sequence QPL
description Cytoplasmic => ECO:0000269|PubMed:26542571
source Swiss-Prot : SWS_FT_FI1

22) chain C
residue 507-518
type TOPO_DOM
sequence FEGSFLVRFISR
description Cytoplasmic => ECO:0000269|PubMed:26542571
source Swiss-Prot : SWS_FT_FI1

23) chain C
residue 592-602
type TOPO_DOM
sequence KNSSYFPGKLR
description Cytoplasmic => ECO:0000269|PubMed:26542571
source Swiss-Prot : SWS_FT_FI1

24) chain C
residue 685-700
type TOPO_DOM
sequence TTLIVSKPERKMVKGS
description Cytoplasmic => ECO:0000269|PubMed:26542571
source Swiss-Prot : SWS_FT_FI1

25) chain C
residue 738-760
type TOPO_DOM
sequence LTVMIQEVKEQR
description Cytoplasmic => ECO:0000269|PubMed:26542571
source Swiss-Prot : SWS_FT_FI1

26) chain C
residue 801-838
type TOPO_DOM
sequence SGIQLFDRILLLFKPPKYHPDVPYVKRVKTWRMHLFTG
description Cytoplasmic => ECO:0000269|PubMed:26542571
source Swiss-Prot : SWS_FT_FI1

27) chain C
residue 664-684
type TRANSMEM
sequence MFASALPALLVFILIFLESQI
description Helical; Name=8 => ECO:0000269|PubMed:26542571
source Swiss-Prot : SWS_FT_FI10

28) chain C
residue 701-719
type TRANSMEM
sequence GFHLDLLLVVGMGGVAALF
description Helical; Name=9 => ECO:0000269|PubMed:26542571
source Swiss-Prot : SWS_FT_FI11

29) chain C
residue 720-737
type TRANSMEM
sequence GMPWLSATTVRSVTHANA
description Discontinuously helical; Name=10 => ECO:0000269|PubMed:26542571
source Swiss-Prot : SWS_FT_FI12

30) chain C
residue 761-781
type TRANSMEM
sequence ISGLLVAVLVGLSILMEPILS
description Helical; Name=11 => ECO:0000269|PubMed:26542571
source Swiss-Prot : SWS_FT_FI13

31) chain C
residue 782-800
type TRANSMEM
sequence RIPLAVLFGIFLYMGVTSL
description Helical; Name=12 => ECO:0000269|PubMed:26542571
source Swiss-Prot : SWS_FT_FI14

32) chain C
residue 590
type SITE
sequence K
description Important for anion transport
source Swiss-Prot : SWS_FT_FI16

33) chain C
residue 681
type SITE
sequence E
description Important for anion-proton cotransport
source Swiss-Prot : SWS_FT_FI17

34) chain C
residue 839-869
type INTRAMEM
sequence IQIICLAVLWVVKSTPASLALPFVLILTVPL
description Discontinuously helical => ECO:0000269|PubMed:26542571
source Swiss-Prot : SWS_FT_FI15


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