eF-site ID 5ndc-A
PDB Code 5ndc
Chain A

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Title Structure of ba3-type cytochrome c oxidase from Thermus thermophilus by serial femtosecond crystallography
Classification OXIDOREDUCTASE
Compound Cytochrome c oxidase subunit 1
Source (A0A1J1EEV7_THETH)
Sequence A:  SRVYEAYPEKKATLYFLVLGFLALIVGSLFGPFQALNYGN
VDAYPLLKRLLPFVQSYYQGLTLHGVLNAIVFTQLFAQAI
MVYLPARELNMRPNMGLMWLSWWMAFIGLVVAALPLLANE
ATVLYTFYPPLKGHWAFYLGASVFVLSTWVSIYIVLDLWR
RWKAANPGKVTPLVTYMAVVFWLMWFLASLGLVLEAVLFL
LPWSFGLVEGVDPLVARTLFWWTGHPIVYFWLLPAYAIIY
TILPKQAGGKLVSDPMARLAFLLFLLLSTPVGFHHQFADP
GIDPTWKMIHSVLTLFVAVPSLMTAFTVAASLEFAGRLRG
GRGLFGWIRALPWDNPAFVAPVLGLLGFIPGGAGGIVNAS
FTLDYVVHNTAWVPGHFHLQVASLVTLTAMGSLYWLLPNL
TGKPISDAQRRLGLAVVWLWFLGMMIMAVGLHWAGLLNVP
RRAYIAQVPDAYPHAAVPMVFNVLAGIVLLVALLLFIYGL
FSVLLSRERKPELAEAPLPFAEVISGPEDRRLVLAMDRIG
FWFAVAAILVVLAYGPTLVQLFGHLNPVPGWRLW
Description


Functional site

1) chain A
residue 233
type
sequence H
description binding site for residue CU A 601
source : AC1

2) chain A
residue 282
type
sequence H
description binding site for residue CU A 601
source : AC1

3) chain A
residue 283
type
sequence H
description binding site for residue CU A 601
source : AC1

4) chain A
residue 39
type
sequence G
description binding site for residue HEM A 602
source : AC2

5) chain A
residue 42
type
sequence Q
description binding site for residue HEM A 602
source : AC2

6) chain A
residue 43
type
sequence A
description binding site for residue HEM A 602
source : AC2

7) chain A
residue 46
type
sequence Y
description binding site for residue HEM A 602
source : AC2

8) chain A
residue 65
type
sequence Y
description binding site for residue HEM A 602
source : AC2

9) chain A
residue 72
type
sequence H
description binding site for residue HEM A 602
source : AC2

10) chain A
residue 76
type
sequence N
description binding site for residue HEM A 602
source : AC2

11) chain A
residue 132
type
sequence L
description binding site for residue HEM A 602
source : AC2

12) chain A
residue 133
type
sequence Y
description binding site for residue HEM A 602
source : AC2

13) chain A
residue 385
type
sequence F
description binding site for residue HEM A 602
source : AC2

14) chain A
residue 386
type
sequence H
description binding site for residue HEM A 602
source : AC2

15) chain A
residue 389
type
sequence V
description binding site for residue HEM A 602
source : AC2

16) chain A
residue 390
type
sequence A
description binding site for residue HEM A 602
source : AC2

17) chain A
residue 394
type
sequence T
description binding site for residue HEM A 602
source : AC2

18) chain A
residue 432
type
sequence M
description binding site for residue HEM A 602
source : AC2

19) chain A
residue 449
type
sequence R
description binding site for residue HEM A 602
source : AC2

20) chain A
residue 450
type
sequence R
description binding site for residue HEM A 602
source : AC2

21) chain A
residue 451
type
sequence A
description binding site for residue HEM A 602
source : AC2

22) chain A
residue 133
type
sequence Y
description binding site for residue HAS A 603
source : AC3

23) chain A
residue 229
type
sequence W
description binding site for residue HAS A 603
source : AC3

24) chain A
residue 236
type
sequence V
description binding site for residue HAS A 603
source : AC3

25) chain A
residue 237
type
sequence Y
description binding site for residue HAS A 603
source : AC3

26) chain A
residue 282
type
sequence H
description binding site for residue HAS A 603
source : AC3

27) chain A
residue 302
type
sequence T
description binding site for residue HAS A 603
source : AC3

28) chain A
residue 310
type
sequence L
description binding site for residue HAS A 603
source : AC3

29) chain A
residue 313
type
sequence A
description binding site for residue HAS A 603
source : AC3

30) chain A
residue 353
type
sequence L
description binding site for residue HAS A 603
source : AC3

31) chain A
residue 360
type
sequence G
description binding site for residue HAS A 603
source : AC3

32) chain A
residue 363
type
sequence G
description binding site for residue HAS A 603
source : AC3

33) chain A
residue 366
type
sequence N
description binding site for residue HAS A 603
source : AC3

34) chain A
residue 367
type
sequence A
description binding site for residue HAS A 603
source : AC3

35) chain A
residue 372
type
sequence D
description binding site for residue HAS A 603
source : AC3

36) chain A
residue 376
type
sequence H
description binding site for residue HAS A 603
source : AC3

37) chain A
residue 384
type
sequence H
description binding site for residue HAS A 603
source : AC3

38) chain A
residue 385
type
sequence F
description binding site for residue HAS A 603
source : AC3

39) chain A
residue 388
type
sequence Q
description binding site for residue HAS A 603
source : AC3

40) chain A
residue 449
type
sequence R
description binding site for residue HAS A 603
source : AC3

41) chain A
residue 213
type
sequence F
description binding site for residue OLC A 604
source : AC4

42) chain A
residue 215
type
sequence L
description binding site for residue OLC A 604
source : AC4

43) chain A
residue 341
type
sequence W
description binding site for residue OLC A 604
source : AC4

44) chain A
residue 426
type
sequence W
description binding site for residue OLC A 604
source : AC4

45) chain A
residue 143
type
sequence W
description binding site for residue OLC A 605
source : AC5

46) chain A
residue 212
type
sequence S
description binding site for residue OLC A 605
source : AC5

47) chain A
residue 111
type
sequence W
description binding site for residue OLC A 606
source : AC6

48) chain A
residue 167
type
sequence W
description binding site for residue OLC A 607
source : AC7

49) chain A
residue 168
type
sequence R
description binding site for residue OLC A 607
source : AC7

50) chain A
residue 531
type
sequence F
description binding site for residue OLC A 607
source : AC7

51) chain A
residue 111
type
sequence W
description binding site for residue OLC A 608
source : AC8

52) chain A
residue 102
type
sequence N
description binding site for residue OLC A 609
source : AC9

53) chain A
residue 472
type
sequence L
description binding site for residue OLC A 609
source : AC9

54) chain A
residue 419
type
sequence R
description binding site for residue OLC A 610
source : AD1

55) chain A
residue 420
type
sequence L
description binding site for residue OLC A 610
source : AD1

56) chain A
residue 341
type
sequence W
description binding site for residue OLC A 611
source : AD2

57) chain A
residue 441
type
sequence W
description binding site for residue OLC C 102
source : AD7

58) chain A
residue 444
type
sequence L
description binding site for residue OLC C 102
source : AD7

59) chain A
residue 385-405
type TRANSMEM
sequence FHLQVASLVTLTAMGSLYWLL
description Helical
source Swiss-Prot : SWS_FT_FI1

60) chain A
residue 420-440
type TRANSMEM
sequence LGLAVVWLWFLGMMIMAVGLH
description Helical
source Swiss-Prot : SWS_FT_FI1

61) chain A
residue 471-491
type TRANSMEM
sequence VLAGIVLLVALLLFIYGLFSV
description Helical
source Swiss-Prot : SWS_FT_FI1

62) chain A
residue 527-547
type TRANSMEM
sequence IGFWFAVAAILVVLAYGPTLV
description Helical
source Swiss-Prot : SWS_FT_FI1

63) chain A
residue 74-94
type TRANSMEM
sequence VLNAIVFTQLFAQAIMVYLPA
description Helical
source Swiss-Prot : SWS_FT_FI1

64) chain A
residue 105-125
type TRANSMEM
sequence LMWLSWWMAFIGLVVAALPLL
description Helical
source Swiss-Prot : SWS_FT_FI1

65) chain A
residue 144-164
type TRANSMEM
sequence AFYLGASVFVLSTWVSIYIVL
description Helical
source Swiss-Prot : SWS_FT_FI1

66) chain A
residue 187-207
type TRANSMEM
sequence VVFWLMWFLASLGLVLEAVLF
description Helical
source Swiss-Prot : SWS_FT_FI1

67) chain A
residue 227-247
type TRANSMEM
sequence LFWWTGHPIVYFWLLPAYAII
description Helical
source Swiss-Prot : SWS_FT_FI1

68) chain A
residue 267-287
type TRANSMEM
sequence LAFLLFLLLSTPVGFHHQFAD
description Helical
source Swiss-Prot : SWS_FT_FI1

69) chain A
residue 300-320
type TRANSMEM
sequence VLTLFVAVPSLMTAFTVAASL
description Helical
source Swiss-Prot : SWS_FT_FI1

70) chain A
residue 345-365
type TRANSMEM
sequence AFVAPVLGLLGFIPGGAGGIV
description Helical
source Swiss-Prot : SWS_FT_FI1

71) chain A
residue 384
type MOD_RES
sequence H
description N-formylmethionine => ECO:0000269|PubMed:11152118
source Swiss-Prot : SWS_FT_FI2

72) chain A
residue 386
type MOD_RES
sequence H
description N-formylmethionine => ECO:0000269|PubMed:11152118
source Swiss-Prot : SWS_FT_FI2

73) chain A
residue 233
type CROSSLNK
sequence H
description 1'-histidyl-3'-tyrosine (His-Tyr)
source Swiss-Prot : SWS_FT_FI5

74) chain A
residue 237
type CROSSLNK
sequence Y
description 1'-histidyl-3'-tyrosine (His-Tyr)
source Swiss-Prot : SWS_FT_FI5

75) chain A
residue 237
type TOPO_DOM
sequence Y
description Periplasmic
source Swiss-Prot : SWS_FT_FI3

76) chain A
residue 384
type catalytic
sequence H
description 735
source MCSA : MCSA1

77) chain A
residue 385
type catalytic
sequence F
description 735
source MCSA : MCSA1

78) chain A
residue 386
type catalytic
sequence H
description 735
source MCSA : MCSA1

79) chain A
residue 449
type catalytic
sequence R
description 735
source MCSA : MCSA1

80) chain A
residue 450
type catalytic
sequence R
description 735
source MCSA : MCSA1

81) chain A
residue 229-283
type prosite
sequence WWTGHPIVYFWLLPAYAIIYTILPKQAGGKLVSDPMARLA
FLLFLLLSTPVGFHH
description COX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WWTGHPiVyfwllpayaiiytilpkqaggklvsdpmarlafllflllstpvgf..HH
source prosite : PS00077


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