eF-site/Summary 5a11-AB

eF-site ID	5a11-AB
PDB Code	5a11
Chain	A, B

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Title	The crystal structure of Ta-TFP, a thiocyanate-forming protein involved in glucosinolate breakdown (space group P21)
Classification	IMMUNE SYSTEM
Compound	THIOCYANATE FORMING PROTEIN
Source	Thlaspi arvense (Field penny-cress) (G1FNI6_THLAR)

Sequence	A:	TLQGEWMKVEQKGGQVPAPRSSHGIAVIGDKLYCFGGEDP PYESIDNDLYVFDFNTHTWSIAPANGDVPKTRVLGTRMVA VGTKLYVFGGRNKQLEFEDFYSYDTVKEEWKFLTKLDEKG GPEARTFHSMTSDENHVYVFGGVSKGGLNATPFRFRTIEA YNIAEGKWAQLPDPGEDFEKRGMAGFLVVQGKLWVFYGFA TANDPKIPTLYGSQDYESNRVHCYDPATQKWTEVETTGFE KPSRRSCFAHAAVGKYIIIFGGEIERDPEAHQGPGTLSRE GFALDTETLVWERYEGGPIKPSNRGWVASTTTTINGKKGL LVHGGKLMTNERTDEMYFFAVNSST
	B:	TLQGEWMKVEQKGGQVPAPRSSHGIAVIGDKLYCFGGEDP PYESIDNDLYVFDFNTHTWSIAPANGDVPKTRVLGTRMVA VGTKLYVFGGRNKQLEFEDFYSYDTVKEEWKFLTKLDEKG GPEARTFHSMTSDENHVYVFGGVSKGGLNATPFRFRTIEA YNIAEGKWAQLPDPGEDFEKRGMAGFLVVQGKLWVFYGFA TANDPKIPTLYGSQDYESNRVHCYDPATQKWTEVETTGFE KPSRRSCFAHAAVGKYIIIFGGEIERDPEAHQGPGTLSRE GFALDTETLVWERYEGGPIKPSNRGWVASTTTTINGKKGL LVHGGKLMTNERTDEMYFFAVNSST

Description

Functional site


1)	chain	A
	residue	157
	type
	sequence	R
	description	BINDING SITE FOR RESIDUE IOD A 1349
	source	: AC1

2)	chain	B
	residue	157
	type
	sequence	R
	description	BINDING SITE FOR RESIDUE IOD B 1349
	source	: AC2

3)	chain	B
	residue	80
	type
	sequence	R
	description	BINDING SITE FOR RESIDUE IOD B 1350
	source	: AC3

4)	chain	A
	residue	80
	type
	sequence	R
	description	BINDING SITE FOR RESIDUE IOD A 1350
	source	: AC4

5)	chain	A
	residue	10
	type
	sequence	M
	description	BINDING SITE FOR RESIDUE IOD A 1351
	source	: AC5

6)	chain	B
	residue	94
	type
	sequence	R
	description	BINDING SITE FOR RESIDUE IOD B 1351
	source	: AC6

7)	chain	B
	residue	148
	type
	sequence	K
	description	BINDING SITE FOR RESIDUE IOD B 1351
	source	: AC6

8)	chain	A
	residue	94
	type	ACT_SITE
	sequence	R
	description	Proton donor => ECO:0000269\|PubMed:26260516, ECO:0000305\|PubMed:23999604, ECO:0000305\|PubMed:28479247, ECO:0000305\|PubMed:30900313
	source	Swiss-Prot : SWS_FT_FI1

9)	chain	B
	residue	94
	type	ACT_SITE
	sequence	R
	description	Proton donor => ECO:0000269\|PubMed:26260516, ECO:0000305\|PubMed:23999604, ECO:0000305\|PubMed:28479247, ECO:0000305\|PubMed:30900313
	source	Swiss-Prot : SWS_FT_FI1

10)	chain	A
	residue	157
	type	ACT_SITE
	sequence	R
	description	Proton donor => ECO:0000269\|PubMed:26260516, ECO:0000305\|PubMed:28479247, ECO:0000305\|PubMed:30900313
	source	Swiss-Prot : SWS_FT_FI2

11)	chain	B
	residue	157
	type	ACT_SITE
	sequence	R
	description	Proton donor => ECO:0000269\|PubMed:26260516, ECO:0000305\|PubMed:28479247, ECO:0000305\|PubMed:30900313
	source	Swiss-Prot : SWS_FT_FI2

12)	chain	A
	residue	220
	type	ACT_SITE
	sequence	E
	description	Proton acceptor => ECO:0000305\|PubMed:30900313
	source	Swiss-Prot : SWS_FT_FI3

13)	chain	B
	residue	220
	type	ACT_SITE
	sequence	E
	description	Proton acceptor => ECO:0000305\|PubMed:30900313
	source	Swiss-Prot : SWS_FT_FI3

14)	chain	A
	residue	46
	type	BINDING
	sequence	E
	description	BINDING => ECO:0000305\|PubMed:23999604
	source	Swiss-Prot : SWS_FT_FI4

15)	chain	A
	residue	310
	type	BINDING
	sequence	V
	description	BINDING => ECO:0000305\|PubMed:23999604
	source	Swiss-Prot : SWS_FT_FI4

16)	chain	B
	residue	46
	type	BINDING
	sequence	E
	description	BINDING => ECO:0000305\|PubMed:23999604
	source	Swiss-Prot : SWS_FT_FI4

17)	chain	B
	residue	310
	type	BINDING
	sequence	V
	description	BINDING => ECO:0000305\|PubMed:23999604
	source	Swiss-Prot : SWS_FT_FI4

18)	chain	A
	residue	94
	type	BINDING
	sequence	R
	description	BINDING => ECO:0000305\|PubMed:23999604, ECO:0000305\|PubMed:26260516, ECO:0000305\|PubMed:28479247, ECO:0000305\|PubMed:30900313
	source	Swiss-Prot : SWS_FT_FI5

19)	chain	A
	residue	266
	type	BINDING
	sequence	E
	description	BINDING => ECO:0000305\|PubMed:23999604, ECO:0000305\|PubMed:26260516, ECO:0000305\|PubMed:28479247, ECO:0000305\|PubMed:30900313
	source	Swiss-Prot : SWS_FT_FI5

20)	chain	A
	residue	270
	type	BINDING
	sequence	D
	description	BINDING => ECO:0000305\|PubMed:23999604, ECO:0000305\|PubMed:26260516, ECO:0000305\|PubMed:28479247, ECO:0000305\|PubMed:30900313
	source	Swiss-Prot : SWS_FT_FI5

21)	chain	A
	residue	274
	type	BINDING
	sequence	H
	description	BINDING => ECO:0000305\|PubMed:23999604, ECO:0000305\|PubMed:26260516, ECO:0000305\|PubMed:28479247, ECO:0000305\|PubMed:30900313
	source	Swiss-Prot : SWS_FT_FI5

22)	chain	B
	residue	94
	type	BINDING
	sequence	R
	description	BINDING => ECO:0000305\|PubMed:23999604, ECO:0000305\|PubMed:26260516, ECO:0000305\|PubMed:28479247, ECO:0000305\|PubMed:30900313
	source	Swiss-Prot : SWS_FT_FI5

23)	chain	B
	residue	266
	type	BINDING
	sequence	E
	description	BINDING => ECO:0000305\|PubMed:23999604, ECO:0000305\|PubMed:26260516, ECO:0000305\|PubMed:28479247, ECO:0000305\|PubMed:30900313
	source	Swiss-Prot : SWS_FT_FI5

24)	chain	B
	residue	270
	type	BINDING
	sequence	D
	description	BINDING => ECO:0000305\|PubMed:23999604, ECO:0000305\|PubMed:26260516, ECO:0000305\|PubMed:28479247, ECO:0000305\|PubMed:30900313
	source	Swiss-Prot : SWS_FT_FI5

25)	chain	B
	residue	274
	type	BINDING
	sequence	H
	description	BINDING => ECO:0000305\|PubMed:23999604, ECO:0000305\|PubMed:26260516, ECO:0000305\|PubMed:28479247, ECO:0000305\|PubMed:30900313
	source	Swiss-Prot : SWS_FT_FI5

26)	chain	A
	residue	129
	type	BINDING
	sequence	T
	description	BINDING => ECO:0000305\|PubMed:28479247
	source	Swiss-Prot : SWS_FT_FI6

27)	chain	B
	residue	129
	type	BINDING
	sequence	T
	description	BINDING => ECO:0000305\|PubMed:28479247
	source	Swiss-Prot : SWS_FT_FI6

28)	chain	A
	residue	130
	type	BINDING
	sequence	F
	description	BINDING => ECO:0000305\|PubMed:23999604, ECO:0000305\|PubMed:26260516, ECO:0000305\|PubMed:30900313
	source	Swiss-Prot : SWS_FT_FI7

29)	chain	B
	residue	130
	type	BINDING
	sequence	F
	description	BINDING => ECO:0000305\|PubMed:23999604, ECO:0000305\|PubMed:26260516, ECO:0000305\|PubMed:30900313
	source	Swiss-Prot : SWS_FT_FI7

30)	chain	A
	residue	157
	type	BINDING
	sequence	R
	description	BINDING => ECO:0000305\|PubMed:26260516, ECO:0000305\|PubMed:28479247, ECO:0000305\|PubMed:30900313
	source	Swiss-Prot : SWS_FT_FI8

31)	chain	A
	residue	309
	type	BINDING
	sequence	W
	description	BINDING => ECO:0000305\|PubMed:26260516, ECO:0000305\|PubMed:28479247, ECO:0000305\|PubMed:30900313
	source	Swiss-Prot : SWS_FT_FI8

32)	chain	B
	residue	157
	type	BINDING
	sequence	R
	description	BINDING => ECO:0000305\|PubMed:26260516, ECO:0000305\|PubMed:28479247, ECO:0000305\|PubMed:30900313
	source	Swiss-Prot : SWS_FT_FI8

33)	chain	B
	residue	309
	type	BINDING
	sequence	W
	description	BINDING => ECO:0000305\|PubMed:26260516, ECO:0000305\|PubMed:28479247, ECO:0000305\|PubMed:30900313
	source	Swiss-Prot : SWS_FT_FI8

34)	chain	A
	residue	269
	type	BINDING
	sequence	R
	description	BINDING => ECO:0000305\|PubMed:23999604, ECO:0000305\|PubMed:28479247
	source	Swiss-Prot : SWS_FT_FI9

35)	chain	B
	residue	269
	type	BINDING
	sequence	R
	description	BINDING => ECO:0000305\|PubMed:23999604, ECO:0000305\|PubMed:28479247
	source	Swiss-Prot : SWS_FT_FI9

36)	chain	A
	residue	45
	type	SITE
	sequence	Y
	description	Essential for catalytic activity => ECO:0000269\|PubMed:30900313
	source	Swiss-Prot : SWS_FT_FI10

37)	chain	B
	residue	45
	type	SITE
	sequence	Y
	description	Essential for catalytic activity => ECO:0000269\|PubMed:30900313
	source	Swiss-Prot : SWS_FT_FI10

38)	chain	A
	residue	154
	type	SITE
	sequence	T
	description	Critical for thiocyanate and epithionitrile formation with allylglucosinolate in the presence of myrosinase => ECO:0000269\|PubMed:30900313
	source	Swiss-Prot : SWS_FT_FI11

39)	chain	B
	residue	154
	type	SITE
	sequence	T
	description	Critical for thiocyanate and epithionitrile formation with allylglucosinolate in the presence of myrosinase => ECO:0000269\|PubMed:30900313
	source	Swiss-Prot : SWS_FT_FI11