eF-site ID 5a11-B
PDB Code 5a11
Chain B

click to enlarge
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 B:  TLQGEWMKVEQKGGQVPAPRSSHGIAVIGDKLYCFGGEDP
PYESIDNDLYVFDFNTHTWSIAPANGDVPKTRVLGTRMVA
VGTKLYVFGGRNKQLEFEDFYSYDTVKEEWKFLTKLDEKG
GPEARTFHSMTSDENHVYVFGGVSKGGLNATPFRFRTIEA
YNIAEGKWAQLPDPGEDFEKRGMAGFLVVQGKLWVFYGFA
TANDPKIPTLYGSQDYESNRVHCYDPATQKWTEVETTGFE
KPSRRSCFAHAAVGKYIIIFGGEIERDPEAHQGPGTLSRE
GFALDTETLVWERYEGGPIKPSNRGWVASTTTTINGKKGL
LVHGGKLMTNERTDEMYFFAVNSST
Description


Functional site

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

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

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

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

5) 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

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

7) 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

8) 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

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

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

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

12) 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

13) 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

14) 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

15) 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

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

17) 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

18) 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

19) 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

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


Display surface

Download
Links