eF-site ID 1lgc-ABCDEFHIJ
PDB Code 1lgc
Chain A, B, C, D, E, F, H, I, J

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Title INTERACTION OF A LEGUME LECTIN WITH THE N2 FRAGMENT OF HUMAN LACTOTRANSFERRIN OR WITH THE ISOLATED BIANTENNARY GLYCOPEPTIDE: ROLE OF THE FUCOSE MOIETY
Classification LECTIN
Compound LEGUME ISOLECTIN II (ALPHA CHAIN)
Source null (LEC2_LATOC)
Sequence A:  TETTSFSITKFGPDQPNLIFQGDGYTTKERLTLTKAVRNT
VGRALYSSPIHIWDSKTGNVANFVTSFTFVIDAPNSYNVA
DGFTFFIAPVDTKPQTGGGYLGVFNSKDYDKTSQTVAVEF
DTFYNTAWDPSNGDRHIGIDVNSIKSINTKSWKLQNGKEA
NVVIAFNGATNVLTVSLTYPN
B:  ETSYTLNEVVPLKEFVPEWVRIGFSATTGAEFAAHEVLSW
YFNSELSVTSS
C:  TETTSFSITKFGPDQPNLIFQGDGYTTKERLTLTKAVRNT
VGRALYSSPIHIWDSKTGNVANFVTSFTFVIDAPNSYNVA
DGFTFFIAPVDTKPQTGGGYLGVFNSKDYDKTSQTVAVEF
DTFYNTAWDPSNGDRHIGIDVNSIKSINTKSWKLQNGKEA
NVVIAFNGATNVLTVSLTYPN
D:  ETSYTLNEVVPLKEFVPEWVRIGFSATTGAEFAAHEVLSW
YFNSELSV
E:  TETTSFSITKFGPDQPNLIFQGDGYTTKERLTLTKAVRNT
VGRALYSSPIHIWDSKTGNVANFVTSFTFVIDAPNSYNVA
DGFTFFIAPVDTKPQTGGGYLGVFNSKDYDKTSQTVAVEF
DTFYNTAWDPSNGDRHIGIDVNSIKSINTKSWKLQNGKEA
NVVIAFNGATNVLTVSLTYPN
F:  TSYTLNEVVPLKEFVPEWVRIGFSATTGAEFAAHEVLSWY
FNSELSV
H:  N
I:  N
J:  NQ
Description (1)  LEGUME ISOLECTIN II (LOL II) COMPLEXED WITH A HUMAN LACTOTRANSFERRIN GLYCOPEPTIDE


Functional site

1) chain A
residue 99
type
sequence G
description MANNOSE (MAN 4) BINDING SITE 1
source : A1

2) chain A
residue 81
type
sequence D
description MANNOSE (MAN 4) BINDING SITE 1
source : A1

3) chain A
residue 125
type
sequence N
description MANNOSE (MAN 4) BINDING SITE 1
source : A1

4) chain B
residue 29
type
sequence G
description MANNOSE (MAN 4) BINDING SITE 1
source : A1

5) chain B
residue 30
type
sequence A
description MANNOSE (MAN 4) BINDING SITE 1
source : A1

6) chain B
residue 31
type
sequence E
description MANNOSE (MAN 4) BINDING SITE 1
source : A1

7) chain B
residue 32
type
sequence F
description FUCOSE (FUC 1) BINDING CAVITY 1
source : B1

8) chain B
residue 31
type
sequence E
description FUCOSE (FUC 1) BINDING CAVITY 1
source : B1

9) chain C
residue 99
type
sequence G
description MANNOSE (MAN 4) BINDING SITE 2
source : A2

10) chain C
residue 81
type
sequence D
description MANNOSE (MAN 4) BINDING SITE 2
source : A2

11) chain C
residue 125
type
sequence N
description MANNOSE (MAN 4) BINDING SITE 2
source : A2

12) chain D
residue 29
type
sequence G
description MANNOSE (MAN 4) BINDING SITE 2
source : A2

13) chain D
residue 30
type
sequence A
description MANNOSE (MAN 4) BINDING SITE 2
source : A2

14) chain D
residue 31
type
sequence E
description MANNOSE (MAN 4) BINDING SITE 2
source : A2

15) chain D
residue 32
type
sequence F
description FUCOSE (FUC 1) BINDING CAVITY 2
source : B2

16) chain D
residue 31
type
sequence E
description FUCOSE (FUC 1) BINDING CAVITY 2
source : B2

17) chain E
residue 99
type
sequence G
description MANNOSE (MAN 4) BINDING SITE 3
source : A3

18) chain E
residue 81
type
sequence D
description MANNOSE (MAN 4) BINDING SITE 3
source : A3

19) chain E
residue 125
type
sequence N
description MANNOSE (MAN 4) BINDING SITE 3
source : A3

20) chain F
residue 29
type
sequence G
description MANNOSE (MAN 4) BINDING SITE 3
source : A3

21) chain F
residue 30
type
sequence A
description MANNOSE (MAN 4) BINDING SITE 3
source : A3

22) chain F
residue 31
type
sequence E
description MANNOSE (MAN 4) BINDING SITE 3
source : A3

23) chain F
residue 32
type
sequence F
description FUCOSE (FUC 1) BINDING CAVITY 3
source : B3

24) chain F
residue 31
type
sequence E
description FUCOSE (FUC 1) BINDING CAVITY 3
source : B3

25) chain A
residue 116-122
type prosite
sequence VAVEFDT
description LECTIN_LEGUME_BETA Legume lectins beta-chain signature. VAVEFDT
source prosite : PS00307

26) chain B
residue 16-25
type prosite
sequence VPEWVRIGFS
description LECTIN_LEGUME_ALPHA Legume lectins alpha-chain signature. VPEWVRIGFS
source prosite : PS00308

27) chain A
residue 125
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI1

28) chain A
residue 129
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI1

29) chain A
residue 136
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI1

30) chain C
residue 119
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI1

31) chain C
residue 121
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI1

32) chain C
residue 123
type BINDING
sequence F
description
source Swiss-Prot : SWS_FT_FI1

33) chain C
residue 125
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI1

34) chain C
residue 129
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI1

35) chain C
residue 136
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI1

36) chain E
residue 119
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI1

37) chain E
residue 121
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI1

38) chain E
residue 123
type BINDING
sequence F
description
source Swiss-Prot : SWS_FT_FI1

39) chain E
residue 125
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI1

40) chain E
residue 129
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI1

41) chain E
residue 136
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI1

42) chain A
residue 119
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI1

43) chain A
residue 121
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI1

44) chain A
residue 123
type BINDING
sequence F
description
source Swiss-Prot : SWS_FT_FI1


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