eF-site ID 6h0f-ABCDEFGHIJKL
PDB Code 6h0f
Chain A, B, C, D, E, F, G, H, I, J, K, L
Title Structure of DDB1-CRBN-pomalidomide complex bound to IKZF1(ZF2)
Classification SIGNALING PROTEIN
Compound DNA damage-binding protein 1,DNA damage-binding protein 1,DNA damage-binding protein 1,DNA damage-binding protein 1
Source (IKZF1_HUMAN)
Sequence A:  MSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLLIAKNTRLE
IYVVTAEGLRPVKEVGMYGKIAVMELFRPKGESKDLLFIL
TAKYNACILEYKQSGESIDIITRAHGNVQDRIGRPSETGI
IGIIDPECRMIGLRLYDGLFKVIPLDRDNKELKAFNIRLE
ELHVIDVKFLYGCQAPTICFVYQDPQGRHVKTYEVSLREK
EFNKGPWKQENVEAEASMVIAVPEPFGGAIIIGQESITYH
NGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRL
FMLLLEKEEQMDGTVTLKDLRVELLGETSIAECLTYLDNG
VVFVGSRLGDSQLVKLNVDSNEQGSYVVAMETFTNLGPIV
DMCVVDLERQGQGQLVTCSGAFKEGSLRIIRNGIKLHIRT
VPLYESPRKICYQEVSQCFGVLSSRIEVQDTSGGTTALRP
SASTQALSSSVSSSKLFSSSTAPHETSFGEEVEVHNLLII
DQHTFEVLHAHQFLQNEYALSLVSCKLGKDPNTYFIVGTA
MVYPEEAEPKQGRIVVFQYSDGKLQTVAEKEVKGAVYSMV
EFNGKLLASINSTVRLYEWTTEKELRTECNHYNNIMALYL
KTKGDFILVGDLMRSVLLLAYKPMEGNFEEIARDFNPNWM
SAVEILDDDNFLGAENAFNLFVCQKDSAATTDEERQHLQE
VGLFHLGEFVNVFCHGSLVMQNLGETSTPTQGSVLFGTVN
GMIGLVTSLSESWYNLLLDMQNRLNKVIKSVGKIEHSFWR
SFHTERKTEPATGFIDGDLIESFLDISRPKMQEVVANLQY
DDGSGMKREATADDLIKVVEELTRIH
B:  GRTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVS
MVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQ
DFGIEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPEC
VLPSTMSAVQLESLNKCQIFPSKPVSREDQCSYKWWQKYQ
KRKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENL
KDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRL
RCELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAA
YVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTV
AQCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPD
TEDEISPDKVILCL
C:  GGRGERPFQCNQCGASFTQKGNLLRHIKLHSG
D:  MSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLLIAKNTRLE
IYVVTAEGLRPVKEVGMYGKIAVMELFRPKGESKDLLFIL
TAKYNACILEYKQSGESIDIITRAHGNVQDRIGRPSETGI
IGIIDPECRMIGLRLYDGLFKVIPLDRDNKELKAFNIRLE
ELHVIDVKFLYGCQAPTICFVYQDPQGRHVKTYEVSLREK
EFNKGPWKQENVEAEASMVIAVPEPFGGAIIIGQESITYH
NGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRL
FMLLLEKEEQMDGTVTLKDLRVELLGETSIAECLTYLDNG
VVFVGSRLGDSQLVKLNVDSNEQGSYVVAMETFTNLGPIV
DMCVVDLERQGQGQLVTCSGAFKEGSLRIIRNGIQKLHIR
TVPLYESPRKICYQEVSQCFGVLSSRIEVQDTSGGTTALR
PSASTQALSSSVSSSKLFSSSTAPHETSFGEEVEVHNLLI
IDQHTFEVLHAHQFLQNEYALSLVSCKLGKDPNTYFIVGT
AMVYPEEAEPKQGRIVVFQYSDGKLQTVAEKEVKGAVYSM
VEFNGKLLASINSTVRLYEWTTEKELRTECNHYNNIMALY
LKTKGDFILVGDLMRSVLLLAYKPMEGNFEEIARDFNPNW
MSAVEILDDDNFLGAENAFNLFVCQKDSAATTDEERQHLQ
EVGLFHLGEFVNVFCHGSLVMQTPTQGSVLFGTVNGMIGL
VTSLSESWYNLLLDMQNRLNKVIKSVGKIEHSFWRSFHTE
RKTEPATGFIDGDLIESFLDISRPKMQEVVANLQYDDGSG
MKREATADDLIKVVEELTRIH
E:  GRTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVS
MVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQ
DFGIEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPEC
VLPSTMSAVQLESLNKCQIFPSKPVSREDQCSYKWWQKYQ
KRKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENL
KDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRL
RCELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAA
YVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTV
AQCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPD
TEDEISPDKVILCL
F:  GGRGERPFQCNQCGASFTQKGNLLRHIKLHSG
G:  MSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLLIAKNTRLE
IYVVTAEGLRPVKEVGMYGKIAVMELFRPKGESKDLLFIL
TAKYNACILEYKQSGESIDIITRAHGNVQDRIGRPSETGI
IGIIDPECRMIGLRLYDGLFKVIPLDRDNKELKAFNIRLE
ELHVIDVKFLYGCQAPTICFVYQDPQGRHVKTYEVSLREK
EFNKGPWKQENVEAEASMVIAVPEPFGGAIIIGQESITYH
NGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRL
FMLLLEKEEQMDGTVTLKDLRVELLGETSIAECLTYLDNG
VVFVGSRLGDSQLVKLNVDSNEQGSYVVAMETFTNLGPIV
DMCVVDLERQGQGQLVTCSGAFKEGSLRIIRNGIKLHIRT
VPLYESPRKICYQEVSQCFGVLSSRIEVQDTSGGTTALRP
SASTQALSSSVSSSKLFSSSTAPHETSFGEEVEVHNLLII
DQHTFEVLHAHQFLQNEYALSLVSCKLGKDPNTYFIVGTA
MVYPEEAEPKQGRIVVFQYSDGKLQTVAEKEVKGAVYSMV
EFNGKLLASINSTVRLYEWTTEKELRTECNHYNNIMALYL
KTKGDFILVGDLMRSVLLLAYKPMEGNFEEIARDFNPNWM
SAVEILDDDNFLGAENAFNLFVCQKDSAATTDEERQHLQE
VGLFHLGEFVNVFCHGSLVMQNLGETSTPTQGSVLFGTVN
GMIGLVTSLSESWYNLLLDMQNRLNKVIKSVGKIEHSFWR
SFHTERKTEPATGFIDGDLIESFLDISRPKMQEVVANLQY
DDGSGMKREATADDLIKVVEELTRIH
H:  GRTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVS
MVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQ
DFGIEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPEC
VLPSTMSAVQLESLNKCQIFPSKPVSREDQCSYKWWQKYQ
KRKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENL
KDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRL
RCELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAA
YVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTV
AQCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPD
TEDEISPDKVILCL
I:  GGRGERPFQCNQCGASFTQKGNLLRHIKLHSG
J:  EENLYFQGGGRMSYNYVVTAQKPTAVNGCVTGHFTSAEDL
NLLIAKNTRLEIYVVTAEGLRPVKEVGMYGKIAVMELFRP
KGESKDLLFILTAKYNACILEYKQSGESIDIITRAHGNVQ
DRIGRPSETGIIGIIDPECRMIGLRLYDGLFKVIPLDRDN
KELKAFNIRLEELHVIDVKFLYGCQAPTICFVYQDPQGRH
VKTYEVSLREKEFNKGPWKQENVEAEASMVIAVPEPFGGA
IIIGQESITYHNGDKYLAIAPPIIKQSTIVCHNRVDPNGS
RYLLGDMEGRLFMLLLEKEEQMDGTVTLKDLRVELLGETS
IAECLTYLDNGVVFVGSRLGDSQLVKLNVDSNEQGSYVVA
METFTNLGPIVDMCVVDLERQGQGQLVTCSGAFKEGSLRI
IRNGIGGGEIQKLHIRTVPLYESPRKICYQEVSQCFGVLS
SRIEVQDTSGGTTALRPSASTQALSSSVSSSKLFSSSTAP
HETSFGEEVEVHNLLIIDQHTFEVLHAHQFLQNEYALSLV
SCKLGKDPNTYFIVGTAMVYPEEAEPKQGRIVVFQYSDGK
LQTVAEKEVKGAVYSMVEFNGKLLASINSTVRLYEWTTEK
ELRTECNHYNNIMALYLKTKGDFILVGDLMRSVLLLAYKP
MEGNFEEIARDFNPNWMSAVEILDDDNFLGAENAFNLFVC
QKDSAATTDEERQHLQEVGLFHLGEFVNVFCHGSLVMQNL
GETSTPTQGSVLFGTVNGMIGLVTSLSESWYNLLLDMQNR
LNKVIKSVGKIEHSFWRSFHTERKTEPATGFIDGDLIESF
LDISRPKMQEVVANLQYDDGSGMKREATADDLIKVVEELT
RIH
K:  GRTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVS
MVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQ
DFGIEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPEC
VLPSTMSAVQLESLNKCQIFPSKPVSREDQCSYKWWQKYQ
KRKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENL
KDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRL
RCELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAA
YVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTV
AQCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPD
TEDEISPDKVILCL
L:  GGRGERPFQCNQCGASFTQKGNLLRHIKLHSG
Description


Functional site

1) chain B
residue 323
type
sequence C
description binding site for residue ZN B 501
source : AC1

2) chain B
residue 326
type
sequence C
description binding site for residue ZN B 501
source : AC1

3) chain B
residue 391
type
sequence C
description binding site for residue ZN B 501
source : AC1

4) chain B
residue 394
type
sequence C
description binding site for residue ZN B 501
source : AC1

5) chain B
residue 351
type
sequence N
description binding site for residue Y70 B 502
source : AC2

6) chain B
residue 352
type
sequence P
description binding site for residue Y70 B 502
source : AC2

7) chain B
residue 353
type
sequence H
description binding site for residue Y70 B 502
source : AC2

8) chain B
residue 377
type
sequence E
description binding site for residue Y70 B 502
source : AC2

9) chain B
residue 378
type
sequence H
description binding site for residue Y70 B 502
source : AC2

10) chain B
residue 380
type
sequence W
description binding site for residue Y70 B 502
source : AC2

11) chain B
residue 386
type
sequence W
description binding site for residue Y70 B 502
source : AC2

12) chain B
residue 400
type
sequence W
description binding site for residue Y70 B 502
source : AC2

13) chain B
residue 402
type
sequence F
description binding site for residue Y70 B 502
source : AC2

14) chain C
residue 146
type
sequence Q
description binding site for residue Y70 B 502
source : AC2

15) chain C
residue 147
type
sequence C
description binding site for residue Y70 B 502
source : AC2

16) chain C
residue 148
type
sequence N
description binding site for residue Y70 B 502
source : AC2

17) chain C
residue 149
type
sequence Q
description binding site for residue Y70 B 502
source : AC2

18) chain C
residue 150
type
sequence C
description binding site for residue Y70 B 502
source : AC2

19) chain C
residue 151
type
sequence G
description binding site for residue Y70 B 502
source : AC2

20) chain C
residue 147
type
sequence C
description binding site for residue ZN C 201
source : AC3

21) chain C
residue 150
type
sequence C
description binding site for residue ZN C 201
source : AC3

22) chain C
residue 163
type
sequence H
description binding site for residue ZN C 201
source : AC3

23) chain C
residue 167
type
sequence H
description binding site for residue ZN C 201
source : AC3

24) chain E
residue 323
type
sequence C
description binding site for residue ZN E 501
source : AC4

25) chain E
residue 326
type
sequence C
description binding site for residue ZN E 501
source : AC4

26) chain E
residue 391
type
sequence C
description binding site for residue ZN E 501
source : AC4

27) chain E
residue 394
type
sequence C
description binding site for residue ZN E 501
source : AC4

28) chain E
residue 351
type
sequence N
description binding site for residue Y70 E 502
source : AC5

29) chain E
residue 352
type
sequence P
description binding site for residue Y70 E 502
source : AC5

30) chain E
residue 353
type
sequence H
description binding site for residue Y70 E 502
source : AC5

31) chain E
residue 377
type
sequence E
description binding site for residue Y70 E 502
source : AC5

32) chain E
residue 378
type
sequence H
description binding site for residue Y70 E 502
source : AC5

33) chain E
residue 380
type
sequence W
description binding site for residue Y70 E 502
source : AC5

34) chain E
residue 386
type
sequence W
description binding site for residue Y70 E 502
source : AC5

35) chain E
residue 400
type
sequence W
description binding site for residue Y70 E 502
source : AC5

36) chain E
residue 402
type
sequence F
description binding site for residue Y70 E 502
source : AC5

37) chain F
residue 146
type
sequence Q
description binding site for residue Y70 E 502
source : AC5

38) chain F
residue 147
type
sequence C
description binding site for residue Y70 E 502
source : AC5

39) chain F
residue 148
type
sequence N
description binding site for residue Y70 E 502
source : AC5

40) chain F
residue 149
type
sequence Q
description binding site for residue Y70 E 502
source : AC5

41) chain F
residue 150
type
sequence C
description binding site for residue Y70 E 502
source : AC5

42) chain F
residue 151
type
sequence G
description binding site for residue Y70 E 502
source : AC5

43) chain F
residue 147
type
sequence C
description binding site for residue ZN F 201
source : AC6

44) chain F
residue 150
type
sequence C
description binding site for residue ZN F 201
source : AC6

45) chain F
residue 163
type
sequence H
description binding site for residue ZN F 201
source : AC6

46) chain F
residue 167
type
sequence H
description binding site for residue ZN F 201
source : AC6

47) chain H
residue 323
type
sequence C
description binding site for residue ZN H 501
source : AC7

48) chain H
residue 326
type
sequence C
description binding site for residue ZN H 501
source : AC7

49) chain H
residue 391
type
sequence C
description binding site for residue ZN H 501
source : AC7

50) chain H
residue 394
type
sequence C
description binding site for residue ZN H 501
source : AC7

51) chain H
residue 351
type
sequence N
description binding site for residue Y70 H 502
source : AC8

52) chain H
residue 352
type
sequence P
description binding site for residue Y70 H 502
source : AC8

53) chain H
residue 353
type
sequence H
description binding site for residue Y70 H 502
source : AC8

54) chain H
residue 377
type
sequence E
description binding site for residue Y70 H 502
source : AC8

55) chain H
residue 378
type
sequence H
description binding site for residue Y70 H 502
source : AC8

56) chain H
residue 379
type
sequence S
description binding site for residue Y70 H 502
source : AC8

57) chain H
residue 380
type
sequence W
description binding site for residue Y70 H 502
source : AC8

58) chain H
residue 386
type
sequence W
description binding site for residue Y70 H 502
source : AC8

59) chain H
residue 400
type
sequence W
description binding site for residue Y70 H 502
source : AC8

60) chain H
residue 402
type
sequence F
description binding site for residue Y70 H 502
source : AC8

61) chain I
residue 146
type
sequence Q
description binding site for residue Y70 H 502
source : AC8

62) chain I
residue 147
type
sequence C
description binding site for residue Y70 H 502
source : AC8

63) chain I
residue 148
type
sequence N
description binding site for residue Y70 H 502
source : AC8

64) chain I
residue 149
type
sequence Q
description binding site for residue Y70 H 502
source : AC8

65) chain I
residue 150
type
sequence C
description binding site for residue Y70 H 502
source : AC8

66) chain I
residue 151
type
sequence G
description binding site for residue Y70 H 502
source : AC8

67) chain I
residue 147
type
sequence C
description binding site for residue ZN I 201
source : AC9

68) chain I
residue 150
type
sequence C
description binding site for residue ZN I 201
source : AC9

69) chain I
residue 163
type
sequence H
description binding site for residue ZN I 201
source : AC9

70) chain I
residue 167
type
sequence H
description binding site for residue ZN I 201
source : AC9

71) chain K
residue 323
type
sequence C
description binding site for residue ZN K 501
source : AD1

72) chain K
residue 326
type
sequence C
description binding site for residue ZN K 501
source : AD1

73) chain K
residue 391
type
sequence C
description binding site for residue ZN K 501
source : AD1

74) chain K
residue 394
type
sequence C
description binding site for residue ZN K 501
source : AD1

75) chain K
residue 351
type
sequence N
description binding site for residue Y70 K 502
source : AD2

76) chain K
residue 352
type
sequence P
description binding site for residue Y70 K 502
source : AD2

77) chain K
residue 353
type
sequence H
description binding site for residue Y70 K 502
source : AD2

78) chain K
residue 377
type
sequence E
description binding site for residue Y70 K 502
source : AD2

79) chain K
residue 378
type
sequence H
description binding site for residue Y70 K 502
source : AD2

80) chain K
residue 380
type
sequence W
description binding site for residue Y70 K 502
source : AD2

81) chain K
residue 386
type
sequence W
description binding site for residue Y70 K 502
source : AD2

82) chain K
residue 400
type
sequence W
description binding site for residue Y70 K 502
source : AD2

83) chain K
residue 402
type
sequence F
description binding site for residue Y70 K 502
source : AD2

84) chain L
residue 146
type
sequence Q
description binding site for residue Y70 K 502
source : AD2

85) chain L
residue 147
type
sequence C
description binding site for residue Y70 K 502
source : AD2

86) chain L
residue 148
type
sequence N
description binding site for residue Y70 K 502
source : AD2

87) chain L
residue 149
type
sequence Q
description binding site for residue Y70 K 502
source : AD2

88) chain L
residue 150
type
sequence C
description binding site for residue Y70 K 502
source : AD2

89) chain L
residue 151
type
sequence G
description binding site for residue Y70 K 502
source : AD2

90) chain L
residue 147
type
sequence C
description binding site for residue ZN L 201
source : AD3

91) chain L
residue 150
type
sequence C
description binding site for residue ZN L 201
source : AD3

92) chain L
residue 163
type
sequence H
description binding site for residue ZN L 201
source : AD3

93) chain L
residue 167
type
sequence H
description binding site for residue ZN L 201
source : AD3

94) chain C
residue 147-167
type prosite
sequence CNQCGASFTQKGNLLRHIKLH
description ZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Cnq..CgasFtqkgnllrHikl..H
source prosite : PS00028

95) chain A
residue 2
type MOD_RES
sequence S
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

96) chain E
residue 378
type MOD_RES
sequence H
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

97) chain E
residue 380
type MOD_RES
sequence W
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

98) chain E
residue 386
type MOD_RES
sequence W
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

99) chain E
residue 391
type MOD_RES
sequence C
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

100) chain E
residue 394
type MOD_RES
sequence C
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

101) chain H
residue 323
type MOD_RES
sequence C
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

102) chain H
residue 326
type MOD_RES
sequence C
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

103) chain H
residue 378
type MOD_RES
sequence H
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

104) chain H
residue 380
type MOD_RES
sequence W
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

105) chain H
residue 386
type MOD_RES
sequence W
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

106) chain D
residue 2
type MOD_RES
sequence S
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

107) chain H
residue 391
type MOD_RES
sequence C
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

108) chain H
residue 394
type MOD_RES
sequence C
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

109) chain K
residue 323
type MOD_RES
sequence C
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

110) chain K
residue 326
type MOD_RES
sequence C
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

111) chain K
residue 378
type MOD_RES
sequence H
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

112) chain K
residue 380
type MOD_RES
sequence W
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

113) chain K
residue 386
type MOD_RES
sequence W
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

114) chain K
residue 391
type MOD_RES
sequence C
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

115) chain K
residue 394
type MOD_RES
sequence C
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

116) chain G
residue 2
type MOD_RES
sequence S
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

117) chain J
residue 2
type MOD_RES
sequence S
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

118) chain B
residue 386
type MOD_RES
sequence W
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

119) chain B
residue 391
type MOD_RES
sequence C
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

120) chain B
residue 394
type MOD_RES
sequence C
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

121) chain E
residue 323
type MOD_RES
sequence C
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

122) chain E
residue 326
type MOD_RES
sequence C
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1


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