eF-site ID 5c0j-ABC
PDB Code 5c0j
Chain A, B, C

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Title HLA-A02 carrying RQFGPDWIVA
Classification IMMUNE SYSTEM
Compound HLA class I histocompatibility antigen, A-2 alpha chain
Source Homo sapiens (Human) (5C0J)
Sequence A:  MGSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSD
AASQRMEPRAPWIEQEGPEYWDGETRKVKAHSQTHRVDLG
TLRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYD
GKDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAY
LEGTCVEWLRRYLENGKETLQRTDAPKTHMTHHAVSDHEA
TLRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDG
TFQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEP
B:  MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDL
LKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA
CRVNHVTLSQPKIVKWDRDM
C:  RQFGPDWIVA
Description


Functional site

1) chain A
residue 14
type
sequence R
description binding site for residue EDO A 301
source : AC1

2) chain A
residue 18
type
sequence G
description binding site for residue EDO A 301
source : AC1

3) chain A
residue 19
type
sequence E
description binding site for residue EDO A 301
source : AC1

4) chain A
residue 11
type
sequence S
description binding site for residue EDO A 302
source : AC2

5) chain A
residue 20
type
sequence P
description binding site for residue EDO A 302
source : AC2

6) chain A
residue 22
type
sequence F
description binding site for residue EDO A 302
source : AC2

7) chain A
residue 71
type
sequence S
description binding site for residue EDO A 302
source : AC2

8) chain A
residue 141
type
sequence Q
description binding site for residue EDO A 303
source : AC3

9) chain A
residue 144
type
sequence K
description binding site for residue EDO A 303
source : AC3

10) chain A
residue 207
type
sequence S
description binding site for residue EDO A 304
source : AC4

11) chain A
residue 236
type
sequence A
description binding site for residue EDO A 304
source : AC4

12) chain A
residue 238
type
sequence D
description binding site for residue EDO A 304
source : AC4

13) chain A
residue 240
type
sequence T
description binding site for residue EDO A 304
source : AC4

14) chain A
residue 242
type
sequence Q
description binding site for residue EDO A 304
source : AC4

15) chain B
residue 12
type
sequence R
description binding site for residue EDO A 304
source : AC4

16) chain A
residue 215
type
sequence L
description binding site for residue EDO A 305
source : AC5

17) chain A
residue 216
type
sequence T
description binding site for residue EDO A 305
source : AC5

18) chain A
residue 217
type
sequence W
description binding site for residue EDO A 305
source : AC5

19) chain A
residue 224
type
sequence Q
description binding site for residue EDO A 305
source : AC5

20) chain A
residue 228
type
sequence T
description binding site for residue EDO A 305
source : AC5

21) chain A
residue 109
type
sequence F
description binding site for residue SO4 A 306
source : AC6

22) chain A
residue 128
type
sequence E
description binding site for residue SO4 A 306
source : AC6

23) chain A
residue 129
type
sequence D
description binding site for residue SO4 A 306
source : AC6

24) chain A
residue 130
type
sequence L
description binding site for residue SO4 A 306
source : AC6

25) chain A
residue 131
type
sequence R
description binding site for residue SO4 A 306
source : AC6

26) chain A
residue 161
type
sequence E
description binding site for residue SO4 A 306
source : AC6

27) chain A
residue 8
type
sequence F
description binding site for residue SO4 A 307
source : AC7

28) chain A
residue 27
type
sequence Y
description binding site for residue SO4 A 307
source : AC7

29) chain A
residue 29
type
sequence D
description binding site for residue SO4 A 307
source : AC7

30) chain A
residue 30
type
sequence D
description binding site for residue SO4 A 307
source : AC7

31) chain B
residue 63
type
sequence Y
description binding site for residue SO4 A 307
source : AC7

32) chain B
residue 83
type
sequence N
description binding site for residue CA B 101
source : AC8

33) chain B
residue 84
type
sequence H
description binding site for residue CA B 101
source : AC8

34) chain B
residue 87
type
sequence L
description binding site for residue CA B 101
source : AC8

35) chain A
residue 234
type
sequence R
description binding site for residue EDO B 102
source : AC9

36) chain A
residue 242
type
sequence Q
description binding site for residue EDO B 102
source : AC9

37) chain B
residue 10
type
sequence Y
description binding site for residue EDO B 102
source : AC9

38) chain B
residue 11
type
sequence S
description binding site for residue EDO B 102
source : AC9

39) chain B
residue 13
type
sequence H
description binding site for residue EDO B 102
source : AC9

40) chain B
residue 14
type
sequence P
description binding site for residue EDO B 102
source : AC9

41) chain A
residue 21
type
sequence R
description binding site for residue EDO B 103
source : AD1

42) chain B
residue 33
type
sequence S
description binding site for residue EDO B 103
source : AD1

43) chain B
residue 34
type
sequence D
description binding site for residue EDO B 103
source : AD1

44) chain A
residue 98
type
sequence M
description binding site for residue EDO B 104
source : AD2

45) chain A
residue 115
type
sequence Q
description binding site for residue EDO B 104
source : AD2

46) chain B
residue 57
type
sequence S
description binding site for residue EDO B 104
source : AD2

47) chain B
residue 58
type
sequence K
description binding site for residue EDO B 104
source : AD2

48) chain B
residue 60
type
sequence W
description binding site for residue EDO B 104
source : AD2

49) chain B
residue 8
type
sequence Q
description binding site for residue GOL B 105
source : AD3

50) chain B
residue 9
type
sequence V
description binding site for residue GOL B 105
source : AD3

51) chain B
residue 93
type
sequence V
description binding site for residue GOL B 105
source : AD3

52) chain B
residue 94
type
sequence K
description binding site for residue GOL B 105
source : AD3

53) chain B
residue 95
type
sequence W
description binding site for residue GOL B 105
source : AD3

54) chain B
residue 96
type
sequence D
description binding site for residue GOL B 105
source : AD3

55) chain B
residue 99
type
sequence M
description binding site for residue GOL B 105
source : AD3

56) chain A
residue 97
type
sequence R
description binding site for residue EDO C 301
source : AD4

57) chain A
residue 147
type
sequence W
description binding site for residue EDO C 301
source : AD4

58) chain C
residue 7
type
sequence W
description binding site for residue EDO C 301
source : AD4

59) chain C
residue 8
type
sequence I
description binding site for residue EDO C 301
source : AD4

60) chain C
residue 7
type
sequence W
description binding site for residue EDO C 302
source : AD5

61) chain C
residue 8
type
sequence I
description binding site for residue EDO C 302
source : AD5

62) chain C
residue 9
type
sequence V
description binding site for residue EDO C 302
source : AD5

63) chain C
residue 3
type
sequence F
description binding site for residue EDO C 303
source : AD6

64) chain C
residue 4
type
sequence G
description binding site for residue EDO C 303
source : AD6

65) chain C
residue 5
type
sequence P
description binding site for residue EDO C 303
source : AD6

66) chain C
residue 6
type
sequence D
description binding site for residue EDO C 303
source : AD6

67) chain A
residue 257-263
type prosite
sequence YTCHVQH
description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCHVQH
source prosite : PS00290

68) chain B
residue 78-84
type prosite
sequence YACRVNH
description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCHVQH
source prosite : PS00290

69) chain B
residue 2
type MOD_RES
sequence Q
description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280
source Swiss-Prot : SWS_FT_FI1

70) chain A
residue 73
type MOD_RES
sequence T
description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280
source Swiss-Prot : SWS_FT_FI1

71) chain A
residue 84
type MOD_RES
sequence Y
description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280
source Swiss-Prot : SWS_FT_FI1

72) chain A
residue 143
type MOD_RES
sequence T
description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280
source Swiss-Prot : SWS_FT_FI1

73) chain A
residue 146
type MOD_RES
sequence K
description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280
source Swiss-Prot : SWS_FT_FI1

74) chain A
residue 171
type MOD_RES
sequence Y
description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280
source Swiss-Prot : SWS_FT_FI1

75) chain B
residue 1
type CARBOHYD
sequence I
description N-linked (Glc) (glycation) isoleucine; in hemodialysis-associated amyloidosis => ECO:0000269|PubMed:7918443
source Swiss-Prot : SWS_FT_FI2

76) chain A
residue 159
type CARBOHYD
sequence Y
description N-linked (Glc) (glycation) isoleucine; in hemodialysis-associated amyloidosis => ECO:0000269|PubMed:7918443
source Swiss-Prot : SWS_FT_FI2

77) chain B
residue 19
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443
source Swiss-Prot : SWS_FT_FI3

78) chain B
residue 41
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443
source Swiss-Prot : SWS_FT_FI3

79) chain B
residue 48
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443
source Swiss-Prot : SWS_FT_FI3

80) chain B
residue 58
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443
source Swiss-Prot : SWS_FT_FI3

81) chain B
residue 91
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443
source Swiss-Prot : SWS_FT_FI3

82) chain B
residue 94
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443
source Swiss-Prot : SWS_FT_FI3

83) chain A
residue 86
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
source Swiss-Prot : SWS_FT_FI4


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