eF-site ID 2w6h-ABCDEFGHI
PDB Code 2w6h
Chain A, B, C, D, E, F, G, H, I
Title Low resolution structures of bovine mitochondrial F1-ATPase during controlled dehydration: Hydration State 4A.
Classification HYDROLASE
Compound ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM, MITOCHONDRIAL
Source ORGANISM_COMMON: BOVINE; ORGANISM_SCIENTIFIC: BOS TAURUS;
Sequence A:  DLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMS
LNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEEL
LGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIPRISVR
EPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTI
INQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDA
DAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKH
ALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHS
RLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVI
SITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAM
KQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVR
LTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITK
FENAFLSHVISQHQALLSKIRTDGKISEESDAKLKEIVTN
FLAGFEA
B:  DLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMS
LNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEEL
LGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIPRISVR
EPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTI
INQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDA
DAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKH
ALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHS
RLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVI
SITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAM
KQVAGTMKLELAQYREVALDAATQQLLSRGVRLTELLKQG
QYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSH
VISQHQALLSKIRTDGKISEESDAKLKEIVTNFLAGFEA
C:  ADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSG
LKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVP
VGEELLGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIP
RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSI
AIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVK
RLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFR
DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDV
FYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYI
PTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAA
QTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLL
SRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEP
SKITKFENAFLSHVISQHQALLSKIRTDGKISEESDAKLK
EIVTNFLAGFEA
D:  TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLE
VAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGP
ETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSV
EQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIME
LINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINL
KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEG
QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATD
MGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAH
LDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHY
DVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRAR
KIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGE
YDHLPEQAFYMVGPIEEAVAKADKLAE
E:  TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLE
VAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGP
ETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSV
EQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIME
LINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINL
KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEG
QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATD
MGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAH
LDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHY
DVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRAR
KIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGE
YDHLPEQAFYMVGPIEEAVAKADKLA
F:  TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLE
VAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGP
ETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSV
EQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIME
LINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINL
KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEG
QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATD
MGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAH
LDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHY
DVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRAR
KIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGE
YDHLPEQAFYMVGPIEEAVAKADKLA
G:  ATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKP
ARVYGVGSLALYEKADIKTPELIIGVSSDRGLCGAIHSSV
AKQMKSEAANLKEVKIIGVGDKIRSILHRTHSDQFLVTFK
EVGRRPPTFGDASVIALELLNSGYEFDEGSIIFNRFRSVI
SYKTEEKPIFSLDTISSAESMSIYDDIDADVLRNYQEYSL
ANIIYYSLKESTTSEQSARMTAMDNASKNASEMIDKLTLT
FNRTRQAVITKELIEIISGAAAL
H:  QMSFTFASPTQVFFNSANVRQVDVPTQTGAFGILAAHVPT
LQVLRPGLVVVHAEDGTTSKYFVSSGSVTVNADSSVQLLA
EEAVTLDMLDLGAAKANLEKAQSELLGAADEATRAEIQIR
IEANEALVKAL
I:  VAYWRQAGLSYIRYSQICAKAVRDALKTEFKANAMKTSGS
TIKIVKV
Description


Functional site

1) chain D
residue 162
type catalytic
sequence K
description 178
source MCSA : MCSA1

2) chain D
residue 188
type catalytic
sequence E
description 178
source MCSA : MCSA1

3) chain D
residue 189
type catalytic
sequence R
description 178
source MCSA : MCSA1

4) chain E
residue 162
type catalytic
sequence K
description 178
source MCSA : MCSA2

5) chain E
residue 188
type catalytic
sequence E
description 178
source MCSA : MCSA2

6) chain E
residue 189
type catalytic
sequence R
description 178
source MCSA : MCSA2

7) chain F
residue 162
type catalytic
sequence K
description 178
source MCSA : MCSA3

8) chain F
residue 188
type catalytic
sequence E
description 178
source MCSA : MCSA3

9) chain F
residue 189
type catalytic
sequence R
description 178
source MCSA : MCSA3

10) chain A
residue 363-372
type prosite
sequence PAINVGLSVS
description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAINVGLSVS
source prosite : PS00152

11) chain D
residue 346-355
type prosite
sequence PAVDPLDSTS
description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAINVGLSVS
source prosite : PS00152

12) chain G
residue 258-271
type prosite
sequence ITKELIEIISGAAA
description ATPASE_GAMMA ATP synthase gamma subunit signature. ITkEliEiisGAaA
source prosite : PS00153

13) chain I
residue 20
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P56382
source Swiss-Prot : SWS_FT_FI1

14) chain I
residue 31
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P56382
source Swiss-Prot : SWS_FT_FI1

15) chain I
residue 36
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P56382
source Swiss-Prot : SWS_FT_FI1

16) chain B
residue 430
type MOD_RES
sequence Q
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P56382
source Swiss-Prot : SWS_FT_FI1

17) chain C
residue 170
type MOD_RES
sequence D
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P56382
source Swiss-Prot : SWS_FT_FI1

18) chain C
residue 430
type MOD_RES
sequence Q
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P56382
source Swiss-Prot : SWS_FT_FI1

19) chain A
residue 161
type MOD_RES
sequence R
description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265
source Swiss-Prot : SWS_FT_FI10

20) chain B
residue 161
type MOD_RES
sequence R
description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265
source Swiss-Prot : SWS_FT_FI10

21) chain C
residue 161
type MOD_RES
sequence R
description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265
source Swiss-Prot : SWS_FT_FI10

22) chain A
residue 391
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P25705
source Swiss-Prot : SWS_FT_FI11

23) chain B
residue 391
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P25705
source Swiss-Prot : SWS_FT_FI11

24) chain C
residue 391
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P25705
source Swiss-Prot : SWS_FT_FI11

25) chain A
residue 33
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine; alternate => ECO:0000250
source Swiss-Prot : SWS_FT_FI12

26) chain B
residue 33
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine; alternate => ECO:0000250
source Swiss-Prot : SWS_FT_FI12

27) chain C
residue 33
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine; alternate => ECO:0000250
source Swiss-Prot : SWS_FT_FI12

28) chain I
residue 43
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P56382
source Swiss-Prot : SWS_FT_FI2

29) chain G
residue 245
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P56382
source Swiss-Prot : SWS_FT_FI2

30) chain F
residue 189
type MOD_RES
sequence R
description N6-acetyllysine => ECO:0000250|UniProtKB:P56382
source Swiss-Prot : SWS_FT_FI2

31) chain G
residue 30
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

32) chain E
residue 472
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

33) chain F
residue 74
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

34) chain F
residue 111
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

35) chain F
residue 209
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

36) chain F
residue 214
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

37) chain F
residue 472
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

38) chain G
residue 172
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

39) chain D
residue 209
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

40) chain D
residue 214
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

41) chain D
residue 472
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

42) chain E
residue 74
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

43) chain E
residue 111
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

44) chain E
residue 209
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

45) chain E
residue 214
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

46) chain G
residue 90
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

47) chain C
residue 22
type MOD_RES
sequence S
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

48) chain C
residue 123
type MOD_RES
sequence S
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

49) chain C
residue 141
type MOD_RES
sequence S
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

50) chain G
residue 129
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

51) chain E
residue 148
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

52) chain E
residue 376
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

53) chain F
residue 148
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

54) chain F
residue 376
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

55) chain B
residue 123
type MOD_RES
sequence S
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

56) chain B
residue 141
type MOD_RES
sequence S
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

57) chain G
residue 121
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI5

58) chain E
residue 262
type MOD_RES
sequence T
description Phosphoserine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI5

59) chain F
residue 262
type MOD_RES
sequence T
description Phosphoserine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI5

60) chain D
residue 365
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P06576
source Swiss-Prot : SWS_FT_FI6

61) chain E
residue 365
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P06576
source Swiss-Prot : SWS_FT_FI6

62) chain F
residue 365
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P06576
source Swiss-Prot : SWS_FT_FI6

63) chain D
residue 383
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

64) chain B
residue 498
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

65) chain C
residue 80
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

66) chain C
residue 83
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

67) chain C
residue 89
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

68) chain C
residue 197
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

69) chain C
residue 498
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

70) chain E
residue 383
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

71) chain F
residue 383
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

72) chain A
residue 197
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

73) chain A
residue 498
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

74) chain B
residue 80
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

75) chain B
residue 83
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

76) chain B
residue 89
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

77) chain B
residue 197
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

78) chain D
residue 430
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P56480
source Swiss-Prot : SWS_FT_FI8

79) chain D
residue 435
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P56480
source Swiss-Prot : SWS_FT_FI8

80) chain E
residue 430
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P56480
source Swiss-Prot : SWS_FT_FI8

81) chain E
residue 435
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P56480
source Swiss-Prot : SWS_FT_FI8

82) chain F
residue 430
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P56480
source Swiss-Prot : SWS_FT_FI8

83) chain F
residue 435
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P56480
source Swiss-Prot : SWS_FT_FI8

84) chain D
residue 56
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

85) chain A
residue 488
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

86) chain A
residue 496
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

87) chain B
residue 118
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

88) chain B
residue 124
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

89) chain B
residue 187
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

90) chain B
residue 196
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

91) chain B
residue 218
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

92) chain B
residue 262
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

93) chain B
residue 384
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

94) chain B
residue 455
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

95) chain E
residue 56
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

96) chain B
residue 463
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

97) chain B
residue 488
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

98) chain B
residue 496
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

99) chain C
residue 118
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

100) chain C
residue 124
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

101) chain C
residue 187
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

102) chain C
residue 196
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

103) chain C
residue 218
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

104) chain C
residue 262
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

105) chain C
residue 384
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

106) chain F
residue 56
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

107) chain C
residue 455
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

108) chain C
residue 463
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

109) chain C
residue 488
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

110) chain C
residue 496
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

111) chain A
residue 196
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

112) chain A
residue 218
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

113) chain A
residue 262
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

114) chain A
residue 384
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

115) chain A
residue 455
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

116) chain A
residue 463
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9


Display surface

Download
Links