eF-site ID 4ayx-A
PDB Code 4ayx
Chain A

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Title STRUCTURE OF THE HUMAN MITOCHONDRIAL ABC TRANSPORTER, ABCB10 (ROD FORM B)
Classification MEMBRANE PROTEIN
Compound ATP-BINDING CASSETTE SUB-FAMILY B MEMBER 10
Source Homo sapiens (Human) (ABCBA_HUMAN)
Sequence A:  LPEARKLLGLAYPERRRLAAAVGFLTMSSVISMSAPFFLG
KIIDVIYTNPTVDYSDNLTRLCLGLSAVFLCGAAANAIRV
YLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELIN
RLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPN
LATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQL
AEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAF
ARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSS
FLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREP
KLPFNEGVILNEKSFQGALEFKNVHFAYPARPEVPIFQDF
SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISL
DGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGAD
DPSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVL
LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQ
EALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYG
KHEELLSKPNG
Description


Functional site

1) chain A
residue 534
type
sequence S
description BINDING SITE FOR RESIDUE MG A 801
source : AC1

2) chain A
residue 575
type
sequence Q
description BINDING SITE FOR RESIDUE MG A 801
source : AC1

3) chain A
residue 658
type
sequence D
description BINDING SITE FOR RESIDUE MG A 801
source : AC1

4) chain A
residue 501
type
sequence Y
description BINDING SITE FOR RESIDUE ACP A 900
source : AC2

5) chain A
residue 509
type
sequence I
description BINDING SITE FOR RESIDUE ACP A 900
source : AC2

6) chain A
residue 529
type
sequence S
description BINDING SITE FOR RESIDUE ACP A 900
source : AC2

7) chain A
residue 530
type
sequence G
description BINDING SITE FOR RESIDUE ACP A 900
source : AC2

8) chain A
residue 531
type
sequence S
description BINDING SITE FOR RESIDUE ACP A 900
source : AC2

9) chain A
residue 532
type
sequence G
description BINDING SITE FOR RESIDUE ACP A 900
source : AC2

10) chain A
residue 533
type
sequence K
description BINDING SITE FOR RESIDUE ACP A 900
source : AC2

11) chain A
residue 534
type
sequence S
description BINDING SITE FOR RESIDUE ACP A 900
source : AC2

12) chain A
residue 535
type
sequence T
description BINDING SITE FOR RESIDUE ACP A 900
source : AC2

13) chain A
residue 575
type
sequence Q
description BINDING SITE FOR RESIDUE ACP A 900
source : AC2

14) chain A
residue 170
type
sequence R
description BINDING SITE FOR RESIDUE GLY A 1717
source : AC3

15) chain A
residue 234
type
sequence Y
description BINDING SITE FOR RESIDUE GLY A 1717
source : AC3

16) chain A
residue 242
type
sequence R
description BINDING SITE FOR RESIDUE GLY A 1717
source : AC3

17) chain A
residue 197
type
sequence D
description BINDING SITE FOR RESIDUE LMT A 1720
source : AC4

18) chain A
residue 200
type
sequence Y
description BINDING SITE FOR RESIDUE LMT A 1720
source : AC4

19) chain A
residue 201
type
sequence T
description BINDING SITE FOR RESIDUE LMT A 1720
source : AC4

20) chain A
residue 218
type
sequence L
description BINDING SITE FOR RESIDUE LMT A 1720
source : AC4

21) chain A
residue 421
type
sequence M
description BINDING SITE FOR RESIDUE LMT A 1720
source : AC4

22) chain A
residue 422
type
sequence G
description BINDING SITE FOR RESIDUE LMT A 1720
source : AC4

23) chain A
residue 427
type
sequence T
description BINDING SITE FOR RESIDUE LMT A 1720
source : AC4

24) chain A
residue 428
type
sequence V
description BINDING SITE FOR RESIDUE LMT A 1720
source : AC4

25) chain A
residue 313
type
sequence N
description BINDING SITE FOR RESIDUE CDL A 1721
source : AC5

26) chain A
residue 313
type
sequence N
description BINDING SITE FOR RESIDUE CDL A 1721
source : AC5

27) chain A
residue 316
type
sequence T
description BINDING SITE FOR RESIDUE CDL A 1721
source : AC5

28) chain A
residue 316
type
sequence T
description BINDING SITE FOR RESIDUE CDL A 1721
source : AC5

29) chain A
residue 317
type
sequence F
description BINDING SITE FOR RESIDUE CDL A 1721
source : AC5

30) chain A
residue 317
type
sequence F
description BINDING SITE FOR RESIDUE CDL A 1721
source : AC5

31) chain A
residue 405
type
sequence S
description BINDING SITE FOR RESIDUE CDL A 1721
source : AC5

32) chain A
residue 405
type
sequence S
description BINDING SITE FOR RESIDUE CDL A 1721
source : AC5

33) chain A
residue 416
type
sequence K
description BINDING SITE FOR RESIDUE CDL A 1721
source : AC5

34) chain A
residue 416
type
sequence K
description BINDING SITE FOR RESIDUE CDL A 1721
source : AC5

35) chain A
residue 405
type
sequence S
description BINDING SITE FOR RESIDUE LMT A 1724
source : AC6

36) chain A
residue 409
type
sequence I
description BINDING SITE FOR RESIDUE LMT A 1724
source : AC6

37) chain A
residue 412
type
sequence S
description BINDING SITE FOR RESIDUE LMT A 1724
source : AC6

38) chain A
residue 415
type
sequence Y
description BINDING SITE FOR RESIDUE LMT A 1724
source : AC6

39) chain A
residue 416
type
sequence K
description BINDING SITE FOR RESIDUE LMT A 1724
source : AC6

40) chain A
residue 420
type
sequence L
description BINDING SITE FOR RESIDUE LMT A 1724
source : AC6

41) chain A
residue 423
type
sequence S
description BINDING SITE FOR RESIDUE LMT A 1724
source : AC6

42) chain A
residue 425
type
sequence H
description BINDING SITE FOR RESIDUE LMT A 1724
source : AC6

43) chain A
residue 184
type
sequence I
description BINDING SITE FOR RESIDUE CDL A 1726
source : AC7

44) chain A
residue 229
type
sequence N
description BINDING SITE FOR RESIDUE CDL A 1726
source : AC7

45) chain A
residue 407
type
sequence N
description BINDING SITE FOR RESIDUE CDL A 1726
source : AC7

46) chain A
residue 527
type BINDING
sequence G
description
source Swiss-Prot : SWS_FT_FI4

47) chain A
residue 237-312
type TOPO_DOM
sequence QTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLS
SDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSP
description Mitochondrial intermembrane => ECO:0000255
source Swiss-Prot : SWS_FT_FI3

48) chain A
residue 429-430
type TOPO_DOM
sequence GE
description Mitochondrial intermembrane => ECO:0000255
source Swiss-Prot : SWS_FT_FI3

49) chain A
residue 265
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI5

50) chain A
residue 582
type MOD_RES
sequence C
description S-glutathionyl cysteine => ECO:0000250|UniProtKB:Q9JI39
source Swiss-Prot : SWS_FT_FI6

51) chain A
residue 171-191
type TRANSMEM
sequence LAAAVGFLTMSSVISMSAPFF
description Helical => ECO:0000255|PROSITE-ProRule:PRU00441
source Swiss-Prot : SWS_FT_FI1

52) chain A
residue 216-236
type TRANSMEM
sequence LGLSAVFLCGAAANAIRVYLM
description Helical => ECO:0000255|PROSITE-ProRule:PRU00441
source Swiss-Prot : SWS_FT_FI1

53) chain A
residue 313-333
type TRANSMEM
sequence NLATFVLSVVPPVSIIAVIYG
description Helical => ECO:0000255|PROSITE-ProRule:PRU00441
source Swiss-Prot : SWS_FT_FI1

54) chain A
residue 408-428
type TRANSMEM
sequence LIVLSVLYKGGLLMGSAHMTV
description Helical => ECO:0000255|PROSITE-ProRule:PRU00441
source Swiss-Prot : SWS_FT_FI1

55) chain A
residue 431-451
type TRANSMEM
sequence LSSFLMYAFWVGISIGGLSSF
description Helical => ECO:0000255|PROSITE-ProRule:PRU00441
source Swiss-Prot : SWS_FT_FI1

56) chain A
residue 192-215
type TOPO_DOM
sequence LGKIIDVIYTNPTVDYSDNLTRLC
description Mitochondrial matrix => ECO:0000255
source Swiss-Prot : SWS_FT_FI2

57) chain A
residue 334-407
type TOPO_DOM
sequence RYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTE
IEKYASKVDHVMQLARKEAFARAGFFGATGLSGN
description Mitochondrial matrix => ECO:0000255
source Swiss-Prot : SWS_FT_FI2

58) chain A
residue 634-648
type prosite
sequence LSGGQKQRIAIARAL
description ABC_TRANSPORTER_1 ABC transporters family signature. LSGGQKQRIAIARAL
source prosite : PS00211


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