eF-site ID 2g63-ABCD
PDB Code 2g63
Chain A, B, C, D

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Title Crystal structure of human dipeptidyl peptidase IV (DPPIV) complexed with cyanopyrrolidine (C5-pro-pro) inhibitor 24b
Classification HYDROLASE
Compound Dipeptidyl peptidase 4
Source Homo sapiens (Human) (DPP4_HUMAN)
Sequence A:  SRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILV
FNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEY
NYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWS
PVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGI
TDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEY
SFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSS
VTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRR
IQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFR
PSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFIT
KGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSD
YTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLP
LYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFII
LNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTV
FRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRL
GTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSM
VLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPED
NLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQ
ISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHF
IKQCFS
B:  SRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILV
FNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEY
NYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWS
PVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGI
TDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEY
SFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSS
VTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRR
IQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFR
PSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFIT
KGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSD
YTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLP
LYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFII
LNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTV
FRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRL
GTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSM
VLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPED
NLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQ
ISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHF
IKQCFS
C:  SRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILV
FNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEY
NYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWS
PVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGI
TDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEY
SFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSS
VTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRR
IQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFR
PSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFIT
KGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSD
YTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLP
LYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFII
LNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTV
FRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRL
GTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSM
VLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPED
NLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQ
ISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHF
IKQCFS
D:  SRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILV
FNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEY
NYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWS
PVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGI
TDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEY
SFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSS
VTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRR
IQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFR
PSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFIT
KGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSD
YTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLP
LYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFII
LNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTV
FRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRL
GTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSM
VLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPED
NLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQ
ISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHF
IKQCFS
Description (1)  Dipeptidyl peptidase 4


Functional site

1) chain B
residue 125
type
sequence R
description BINDING SITE FOR RESIDUE AAF B 800
source : AC1

2) chain B
residue 205
type
sequence E
description BINDING SITE FOR RESIDUE AAF B 800
source : AC1

3) chain B
residue 206
type
sequence E
description BINDING SITE FOR RESIDUE AAF B 800
source : AC1

4) chain B
residue 547
type
sequence Y
description BINDING SITE FOR RESIDUE AAF B 800
source : AC1

5) chain B
residue 553
type
sequence Q
description BINDING SITE FOR RESIDUE AAF B 800
source : AC1

6) chain B
residue 630
type
sequence S
description BINDING SITE FOR RESIDUE AAF B 800
source : AC1

7) chain B
residue 631
type
sequence Y
description BINDING SITE FOR RESIDUE AAF B 800
source : AC1

8) chain B
residue 656
type
sequence V
description BINDING SITE FOR RESIDUE AAF B 800
source : AC1

9) chain B
residue 662
type
sequence Y
description BINDING SITE FOR RESIDUE AAF B 800
source : AC1

10) chain B
residue 666
type
sequence Y
description BINDING SITE FOR RESIDUE AAF B 800
source : AC1

11) chain B
residue 710
type
sequence N
description BINDING SITE FOR RESIDUE AAF B 800
source : AC1

12) chain A
residue 547
type catalytic
sequence Y
description 169
source MCSA : MCSA1

13) chain A
residue 630
type catalytic
sequence S
description 169
source MCSA : MCSA1

14) chain A
residue 631
type catalytic
sequence Y
description 169
source MCSA : MCSA1

15) chain A
residue 708
type catalytic
sequence D
description 169
source MCSA : MCSA1

16) chain A
residue 740
type catalytic
sequence H
description 169
source MCSA : MCSA1

17) chain B
residue 547
type catalytic
sequence Y
description 169
source MCSA : MCSA2

18) chain B
residue 630
type catalytic
sequence S
description 169
source MCSA : MCSA2

19) chain B
residue 631
type catalytic
sequence Y
description 169
source MCSA : MCSA2

20) chain B
residue 708
type catalytic
sequence D
description 169
source MCSA : MCSA2

21) chain B
residue 740
type catalytic
sequence H
description 169
source MCSA : MCSA2

22) chain C
residue 547
type catalytic
sequence Y
description 169
source MCSA : MCSA3

23) chain C
residue 630
type catalytic
sequence S
description 169
source MCSA : MCSA3

24) chain C
residue 631
type catalytic
sequence Y
description 169
source MCSA : MCSA3

25) chain C
residue 708
type catalytic
sequence D
description 169
source MCSA : MCSA3

26) chain C
residue 740
type catalytic
sequence H
description 169
source MCSA : MCSA3

27) chain D
residue 547
type catalytic
sequence Y
description 169
source MCSA : MCSA4

28) chain D
residue 630
type catalytic
sequence S
description 169
source MCSA : MCSA4

29) chain D
residue 631
type catalytic
sequence Y
description 169
source MCSA : MCSA4

30) chain D
residue 708
type catalytic
sequence D
description 169
source MCSA : MCSA4

31) chain D
residue 740
type catalytic
sequence H
description 169
source MCSA : MCSA4

32) chain A
residue 605-635
type prosite
sequence DQIEAARQFSKMGFVDNKRIAIWGWSYGGYV
description PRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DqieAarqFskmgfvdnkriaiwGwSyGGYV
source prosite : PS00708

33) chain A
residue 630
type ACT_SITE
sequence S
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1

34) chain D
residue 630
type ACT_SITE
sequence S
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1

35) chain D
residue 708
type ACT_SITE
sequence D
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1

36) chain D
residue 740
type ACT_SITE
sequence H
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1

37) chain A
residue 708
type ACT_SITE
sequence D
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1

38) chain A
residue 740
type ACT_SITE
sequence H
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1

39) chain B
residue 630
type ACT_SITE
sequence S
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1

40) chain B
residue 708
type ACT_SITE
sequence D
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1

41) chain B
residue 740
type ACT_SITE
sequence H
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1

42) chain C
residue 630
type ACT_SITE
sequence S
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1

43) chain C
residue 708
type ACT_SITE
sequence D
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1

44) chain C
residue 740
type ACT_SITE
sequence H
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1

45) chain A
residue 85
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI2

46) chain A
residue 229
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI2

47) chain B
residue 85
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI2

48) chain B
residue 229
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI2

49) chain C
residue 85
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI2

50) chain C
residue 229
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI2

51) chain D
residue 85
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI2

52) chain D
residue 229
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI2

53) chain A
residue 92
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI3

54) chain B
residue 92
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI3

55) chain C
residue 92
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI3

56) chain D
residue 92
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI3

57) chain A
residue 150
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI4

58) chain B
residue 150
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI4

59) chain C
residue 150
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI4

60) chain D
residue 150
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI4

61) chain A
residue 219
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI5

62) chain B
residue 219
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI5

63) chain C
residue 219
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI5

64) chain D
residue 219
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI5

65) chain A
residue 281
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI6

66) chain B
residue 281
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI6

67) chain C
residue 281
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI6

68) chain D
residue 281
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI6

69) chain A
residue 321
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI7

70) chain B
residue 321
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI7

71) chain C
residue 321
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI7

72) chain D
residue 321
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI7

73) chain A
residue 520
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI8

74) chain B
residue 520
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI8

75) chain C
residue 520
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI8

76) chain D
residue 520
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI8

77) chain A
residue 685
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
source Swiss-Prot : SWS_FT_FI9

78) chain B
residue 685
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
source Swiss-Prot : SWS_FT_FI9

79) chain C
residue 685
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
source Swiss-Prot : SWS_FT_FI9

80) chain D
residue 685
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
source Swiss-Prot : SWS_FT_FI9


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