eF-site ID 1w72-ABCDEFHILM
PDB Code 1w72
Chain A, B, C, D, E, F, H, I, L, M

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Title Crystal structure of HLA-A1:MAGE-A1 in complex with Fab-Hyb3
Classification IMMUNE SYSTEM
Compound HLA CLASS I HISTOCOMPATIBILITY ANTIGEN
Source Homo sapiens (Human) (1W72)
Sequence A:  GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDA
ASQKMEPRAPWIEQEGPEYWDQETRNMKAHSQTDRANLGT
LRGYYNQSEDGSHTIQIMYGCDVGPDGRFLRGYRQDAYDG
KDYIALNEDLRSWTAADMAAQITKRKWEAVHAAEQRRVYL
EGRCVDGLRRYLENGKETLQRTDPPKTHMTHHPISDHEAT
LRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT
FQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRW
B:  MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDL
LKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA
CRVNHVTLSQPKIVKWDRDM
C:  EADPTGHSY
D:  GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDA
ASQKMEPRAPWIEQEGPEYWDQETRNMKAHSQTDRANLGT
LRGYYNQSEDGSHTIQIMYGCDVGPDGRFLRGYRQDAYDG
KDYIALNEDLRSWTAADMAAQITKRKWEAVHAAEQRRVYL
EGRCVDGLRRYLENGKETLQRTDPPKTHMTHHPISDHEAT
LRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT
FQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRW
E:  MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDL
LKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA
CRVNHVTLSQPKIVKWDRDM
F:  EADPTGHSY
H:  EVQLVESGGGLVQPGRSLRLSCAASGFTFDDYAMHWVRQA
PGKGLEWVSGISWNSGSIGYADSVKGRFTISRDNAKNSLY
LQMNSLRAEDTAVYYCARGRGFHYYYYGMDIWGQGTTVTV
SSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVT
VSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGT
QTYICNVNHKPSNTKVDKKVEPK
I:  EVQLVESGGGLVQPGRSLRLSCAASGFTFDDYAMHWVRQA
PGKGLEWVSGISWNSGSIGYADSVKGRFTISRDNAKNSLY
LQMNSLRAEDTAVYYCARGRGFHYYYYGMDIWGQGTTVTV
SSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVT
VSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGT
QTYICNVNHKPSNTKVDKKVEPK
L:  SYVLTQPPSVSVAPGQTARITCGGNNIGSRSVHWYQQKPG
QAPVLVVYDDSDRPSGIPERFSGSNSGNMATLTISRVEAG
DEADYYCQVWDSRTDHWVFGGGTDLTVLGQPKAAPSVTLF
PPSSEELQANKATLVCLISDFYPGAVTVAWKADGSPVKAG
VETTKPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHE
GSTVEKTVAP
M:  SYVLTQPPSVSVAPGQTARITCGGNNIGSRSVHWYQQKPG
QAPVLVVYDDSDRPSGIPERFSGSNSGNMATLTISRVEAG
DEADYYCQVWDSRTDHWVFGGGTDLTVLGQPKAAPSVTLF
PPSSEELQANKATLVCLISDFYPGAVTVAWKADGSPVKAG
VETTKPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHE
GSTVEKTVAP
Description


Functional site

1) chain A
residue 178
type
sequence T
description BINDING SITE FOR RESIDUE GOL A1275
source : AC1

2) chain A
residue 181
type
sequence R
description BINDING SITE FOR RESIDUE GOL A1275
source : AC1

3) chain A
residue 183
type
sequence D
description BINDING SITE FOR RESIDUE GOL A1275
source : AC1

4) chain A
residue 209
type
sequence Y
description BINDING SITE FOR RESIDUE GOL A1275
source : AC1

5) chain A
residue 181
type
sequence R
description BINDING SITE FOR RESIDUE GOL A1276
source : AC2

6) chain A
residue 182
type
sequence T
description BINDING SITE FOR RESIDUE GOL A1276
source : AC2

7) chain I
residue 145
type
sequence K
description BINDING SITE FOR RESIDUE GOL I1229
source : AC3

8) chain I
residue 179
type
sequence Q
description BINDING SITE FOR RESIDUE GOL I1229
source : AC3

9) chain I
residue 186
type
sequence S
description BINDING SITE FOR RESIDUE GOL I1229
source : AC3

10) chain M
residue 160
type
sequence E
description BINDING SITE FOR RESIDUE GOL I1229
source : AC3

11) chain M
residue 178
type
sequence Y
description BINDING SITE FOR RESIDUE GOL I1229
source : AC3

12) chain M
residue 180
type
sequence S
description BINDING SITE FOR RESIDUE GOL I1229
source : AC3

13) chain M
residue 37
type
sequence Q
description BINDING SITE FOR RESIDUE GOL M1212
source : AC4

14) chain M
residue 39
type
sequence K
description BINDING SITE FOR RESIDUE GOL M1212
source : AC4

15) chain M
residue 59
type
sequence P
description BINDING SITE FOR RESIDUE GOL M1212
source : AC4

16) chain M
residue 62
type
sequence F
description BINDING SITE FOR RESIDUE GOL M1212
source : AC4

17) chain M
residue 81
type
sequence G
description BINDING SITE FOR RESIDUE GOL M1212
source : AC4

18) chain M
residue 82
type
sequence D
description BINDING SITE FOR RESIDUE GOL M1212
source : AC4

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

20) chain D
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 D
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

23) chain D
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

24) chain D
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

25) chain E
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

26) 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

27) 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

28) 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

29) 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

30) chain D
residue 7
type MOD_RES
sequence Y
description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280
source Swiss-Prot : SWS_FT_FI1

31) chain D
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

32) chain D
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

33) 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

34) chain E
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

35) chain D
residue 116
type CARBOHYD
sequence D
description N-linked (Glc) (glycation) isoleucine; in hemodialysis-associated amyloidosis => ECO:0000269|PubMed:7918443
source Swiss-Prot : SWS_FT_FI2

36) chain D
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

37) 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

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

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

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

41) 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

42) 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

43) 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

44) 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

45) 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

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

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

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

49) chain H
residue 206-212
type prosite
sequence YICNVNH
description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YICNVNH
source prosite : PS00290

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

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

52) chain L
residue 192-198
type prosite
sequence YSCQVTH
description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YICNVNH
source prosite : PS00290


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