eF-site ID 5c0b-I
PDB Code 5c0b
Chain I

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Title 1E6 TCR in complex with HLA-A02 carrying RQFGPDFPTI
Classification IMMUNE SYSTEM
Compound HLA class I histocompatibility antigen, A-2 alpha chain
Source Homo sapiens (Human) (5C0B)
Sequence I:  EVEQDPGPLSVPEGAIVSLNCTYSNSAFQYFMWYRQYSRK
GPELLMYTYSSGNKEDGRFTAQVDKSSKYISLFIRDSQPS
DSATYLCAMRGDSSYKLIFGSGTRLLVRPDIQNPDPAVYQ
LRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLD
MRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPS
Description


Functional site

1) chain I
residue 71
type
sequence Y
description binding site for residue EDO D 301
source : AE1

2) chain I
residue 77
type
sequence R
description binding site for residue EDO D 302
source : AE2

3) chain I
residue 55
type
sequence N
description binding site for residue EDO D 303
source : AE3

4) chain I
residue 64
type
sequence Q
description binding site for residue EDO D 303
source : AE3

5) chain I
residue 65
type
sequence V
description binding site for residue EDO D 303
source : AE3

6) chain I
residue 66
type
sequence D
description binding site for residue EDO D 303
source : AE3

7) chain I
residue 13
type
sequence V
description binding site for residue EDO D 306
source : AE6

8) chain I
residue 18
type
sequence I
description binding site for residue EDO D 306
source : AE6

9) chain I
residue 19
type
sequence V
description binding site for residue EDO D 306
source : AE6

10) chain I
residue 20
type
sequence S
description binding site for residue EDO D 306
source : AE6

11) chain I
residue 92
type
sequence R
description binding site for residue EDO I 301
source : AH9

12) chain I
residue 97
type
sequence Y
description binding site for residue EDO I 301
source : AH9

13) chain I
residue 99
type
sequence L
description binding site for residue EDO I 301
source : AH9

14) chain I
residue 59
type
sequence G
description binding site for residue EDO I 302
source : AI1

15) chain I
residue 60
type
sequence R
description binding site for residue EDO I 302
source : AI1

16) chain I
residue 77
type
sequence R
description binding site for residue EDO I 302
source : AI1

17) chain I
residue 112
type
sequence D
description binding site for residue EDO I 303
source : AI2

18) chain I
residue 113
type
sequence I
description binding site for residue EDO I 303
source : AI2

19) chain I
residue 140
type
sequence D
description binding site for residue EDO I 303
source : AI2

20) chain I
residue 141
type
sequence S
description binding site for residue EDO I 303
source : AI2

21) chain I
residue 142
type
sequence Q
description binding site for residue EDO I 303
source : AI2

22) chain I
residue 179
type
sequence K
description binding site for residue EDO I 304
source : AI3

23) chain I
residue 180
type
sequence S
description binding site for residue EDO I 304
source : AI3

24) chain I
residue 60
type
sequence R
description binding site for residue EDO I 305
source : AI4

25) chain I
residue 16
type
sequence G
description binding site for residue EDO I 306
source : AI5

26) chain I
residue 18
type
sequence I
description binding site for residue EDO I 306
source : AI5

27) chain I
residue 77
type
sequence R
description binding site for residue EDO I 306
source : AI5

28) chain I
residue 78
type
sequence D
description binding site for residue EDO I 306
source : AI5

29) chain I
residue 95
type
sequence S
description binding site for residue EDO I 307
source : AI6

30) chain I
residue 12
type
sequence S
description binding site for residue GOL I 308
source : AI7

31) chain I
residue 13
type
sequence V
description binding site for residue GOL I 308
source : AI7

32) chain I
residue 88
type
sequence L
description binding site for residue PG4 J 308
source : AJ6

33) chain I
residue 102
type
sequence G
description binding site for residue PG4 J 308
source : AJ6

34) chain I
residue 103
type
sequence S
description binding site for residue PG4 J 308
source : AJ6

35) chain I
residue 144
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI2

36) chain I
residue 178
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI2

37) chain I
residue 189
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
source Swiss-Prot : SWS_FT_FI3


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