eF-site ID 5grg-ABCD
PDB Code 5grg
Chain A, B, C, D

click to enlarge
Title Crystal structure of dual peptide from EBV in complex with HLA-A*11:01
Classification IMMUNE SYSTEM
Compound HLA class I histocompatibility antigen, A-11 alpha chain
Source Homo sapiens (Human) (5GRG)
Sequence A:  GSHSMRYFYTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDA
ASQRMEPRAPWIEQEGPEYWDQETRNVKAQSQTDRVDLGT
LRGYYNQSEDGSHTIQIMYGCDVGPDGRFLRGYRQDAYDG
KDYIALNEDLRSWTAADMAAQITKRKWEAAHAAEQQRAYL
EGRCVEWLRRYLENGKETLQRTDPPKTHMTHHPISDHEAT
LRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT
FQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRW
B:  IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLL
KNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC
RVNHVTLSQPKIVKWDRDM
C:  SSCSSC
D:  PLSK
Description


Functional site

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

2) chain A
residue 30
type
sequence D
description binding site for residue GOL A 301
source : AC1

3) chain B
residue 63
type
sequence Y
description binding site for residue GOL A 301
source : AC1

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

5) chain A
residue 189
type
sequence M
description binding site for residue GOL A 302
source : AC2

6) chain B
residue 81
type
sequence R
description binding site for residue GOL A 302
source : AC2

7) chain B
residue 90
type
sequence P
description binding site for residue GOL A 302
source : AC2

8) chain B
residue 92
type
sequence I
description binding site for residue GOL A 302
source : AC2

9) chain A
residue 191
type
sequence H
description binding site for residue GOL B 101
source : AC3

10) chain A
residue 192
type
sequence H
description binding site for residue GOL B 101
source : AC3

11) chain B
residue 34
type
sequence D
description binding site for residue GOL B 101
source : AC3

12) chain B
residue 83
type
sequence N
description binding site for residue GOL B 101
source : AC3

13) chain B
residue 84
type
sequence H
description binding site for residue GOL B 101
source : AC3

14) chain B
residue 85
type
sequence V
description binding site for residue GOL B 101
source : AC3

15) chain A
residue 21
type
sequence R
description binding site for residue GOL B 102
source : AC4

16) chain B
residue 33
type
sequence S
description binding site for residue GOL B 102
source : AC4

17) chain B
residue 35
type
sequence I
description binding site for residue GOL B 102
source : AC4

18) chain B
residue 51
type
sequence H
description binding site for residue GOL B 102
source : AC4

19) chain B
residue 66
type
sequence Y
description binding site for residue GOL B 102
source : AC4

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

21) 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

22) 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

23) 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

24) 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

25) 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

26) 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

27) 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

28) 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

29) 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

30) 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

31) 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

32) 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

33) 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

34) 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

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

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


Display surface

Download
Links