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

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Title Human Leukocyte Antigen presenting ILGKFLHRL
Classification IMMUNE SYSTEM
Compound HLA class I histocompatibility antigen, A-2 alpha chain
Source Homo sapiens (Human) (5MEO)
Sequence A:  GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDA
ASQRMEPRAPWIEQEGPEYWDGETRKVKAHSQTHRVDLGT
LRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYDG
KDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYL
EGTCVEWLRRYLENGKETLQRTDAPKTHMTHHAVSDHEAT
LRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT
FQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEP
Description


Functional site

1) chain A
residue 8
type
sequence F
description binding site for residue EDO A 301
source : AC1

2) chain A
residue 29
type
sequence D
description binding site for residue EDO A 301
source : AC1

3) chain A
residue 188
type
sequence H
description binding site for residue EDO A 302
source : AC2

4) chain A
residue 190
type
sequence T
description binding site for residue EDO A 302
source : AC2

5) chain A
residue 204
type
sequence W
description binding site for residue EDO A 302
source : AC2

6) chain A
residue 17
type
sequence R
description binding site for residue EDO A 303
source : AC3

7) chain A
residue 121
type
sequence K
description binding site for residue EDO A 303
source : AC3

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

9) chain A
residue 20
type
sequence P
description binding site for residue EDO A 304
source : AC4

10) chain A
residue 21
type
sequence R
description binding site for residue EDO A 304
source : AC4

11) chain A
residue 38
type
sequence S
description binding site for residue EDO A 304
source : AC4

12) chain A
residue 39
type
sequence D
description binding site for residue EDO A 304
source : AC4

13) chain A
residue 85
type
sequence Y
description binding site for residue EDO A 305
source : AC5

14) chain A
residue 121
type
sequence K
description binding site for residue EDO A 305
source : AC5

15) chain A
residue 122
type
sequence D
description binding site for residue EDO A 305
source : AC5

16) chain A
residue 137
type
sequence D
description binding site for residue EDO A 305
source : AC5

17) chain A
residue 76
type
sequence V
description binding site for residue EDO A 306
source : AC6

18) chain A
residue 79
type
sequence G
description binding site for residue EDO A 306
source : AC6

19) chain A
residue 80
type
sequence T
description binding site for residue EDO A 306
source : AC6

20) chain A
residue 55
type
sequence E
description binding site for residue EDO A 307
source : AC7

21) chain A
residue 56
type
sequence G
description binding site for residue EDO A 307
source : AC7

22) chain A
residue 57
type
sequence P
description binding site for residue EDO A 307
source : AC7

23) chain A
residue 60
type
sequence W
description binding site for residue EDO A 307
source : AC7

24) chain A
residue 107
type
sequence W
description binding site for residue EDO A 308
source : AC8

25) chain A
residue 173
type
sequence E
description binding site for residue EDO A 308
source : AC8

26) chain A
residue 176
type
sequence K
description binding site for residue EDO A 308
source : AC8

27) chain A
residue 180
type
sequence Q
description binding site for residue EDO A 308
source : AC8

28) chain A
residue 122
type
sequence D
description binding site for residue EDO A 309
source : AC9

29) chain A
residue 13
type
sequence S
description binding site for residue EDO A 310
source : AD1

30) chain A
residue 14
type
sequence R
description binding site for residue EDO A 310
source : AD1

31) chain A
residue 17
type
sequence R
description binding site for residue EDO A 310
source : AD1

32) chain A
residue 92
type
sequence S
description binding site for residue EDO A 310
source : AD1

33) chain A
residue 35
type
sequence R
description binding site for residue GOL A 311
source : AD2

34) chain A
residue 40
type
sequence A
description binding site for residue GOL A 311
source : AD2

35) chain A
residue 41
type
sequence A
description binding site for residue GOL A 311
source : AD2

36) chain A
residue 88
type
sequence S
description binding site for residue GOL A 311
source : AD2

37) chain A
residue 87
type
sequence Q
description binding site for residue GOL A 312
source : AD3

38) chain A
residue 88
type
sequence S
description binding site for residue GOL A 312
source : AD3

39) chain A
residue 93
type
sequence H
description binding site for residue GOL A 312
source : AD3

40) chain A
residue 16
type
sequence G
description binding site for residue GOL A 313
source : AD4

41) chain A
residue 17
type
sequence R
description binding site for residue GOL A 313
source : AD4

42) chain A
residue 18
type
sequence G
description binding site for residue GOL A 313
source : AD4

43) chain A
residue 219
type
sequence R
description binding site for residue SO4 A 314
source : AD5

44) chain A
residue 256
type
sequence R
description binding site for residue SO4 A 314
source : AD5

45) chain A
residue 21
type
sequence R
description binding site for residue SO4 A 315
source : AD6

46) chain A
residue 98
type
sequence M
description binding site for residue EDO B 301
source : AD7

47) chain A
residue 115
type
sequence Q
description binding site for residue EDO B 301
source : AD7

48) chain A
residue 206
type
sequence L
description binding site for residue EDO B 302
source : AD8

49) chain A
residue 234
type
sequence R
description binding site for residue EDO B 302
source : AD8

50) chain A
residue 242
type
sequence Q
description binding site for residue EDO B 302
source : AD8

51) chain A
residue 234
type
sequence R
description binding site for residue EDO B 303
source : AD9

52) chain A
residue 138
type
sequence M
description binding site for residue GOL B 306
source : AE3

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

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

55) 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

56) 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

57) 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

58) 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

59) 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

60) 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


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