eF-site ID 2vce-A
PDB Code 2vce
Chain A

click to enlarge
Title Characterization and engineering of the bifunctional N- and O- glucosyltransferase involved in xenobiotic metabolism in plants
Classification TRANSFERASE
Compound HYDROQUINONE GLUCOSYLTRANSFERASE
Source null (HQGT_ARATH)
Sequence A:  TPHVAIIPSPGMGHLIPLVEFAKRLVHLHGLTVTFVIAGE
GPPSKAQRTVLDSLPSSISSVFLPPVDLTDLSSSTRIESR
ISLTVTRSNPELRKVFDSFVEGGRLPTALVVDLFGTDAFD
VAVEFHVPPYIFYPTTANVLSFFLHLPKLDETVSCEFREL
TEPLMLPGCVPVAGKDFLDPAQDRKDDAYKWLLHNTKRYK
EAEGILVNTFFELEPNAIKALQEPGLDKPPVYPVGPLVNI
GKQEASECLKWLDNQPLGSVLYVSFGSGGTLTCEQLNELA
LGLADSEQRFLWVIRSPSGIANSSYFQTDPLTFLPPGFLE
RTKKRGFVIPFWAPQAQVLAHPSTGGFLTHCGWNSTLESV
VSGIPLIAWPLYAEQKMNAVLLSEDIRAALRPRAGDDGLV
RREEVARVVKGLMEGEEGKGVRNKMKELKEAACRVLKDDG
TSTKALSLVALKWKAHKKELEQ
Description


Functional site

1) chain A
residue 18
type
sequence G
description BINDING SITE FOR RESIDUE U2F A1477
source : AC1

2) chain A
residue 21
type
sequence I
description BINDING SITE FOR RESIDUE U2F A1477
source : AC1

3) chain A
residue 139
type
sequence P
description BINDING SITE FOR RESIDUE U2F A1477
source : AC1

4) chain A
residue 276
type
sequence G
description BINDING SITE FOR RESIDUE U2F A1477
source : AC1

5) chain A
residue 277
type
sequence S
description BINDING SITE FOR RESIDUE U2F A1477
source : AC1

6) chain A
residue 303
type
sequence V
description BINDING SITE FOR RESIDUE U2F A1477
source : AC1

7) chain A
residue 346
type
sequence W
description BINDING SITE FOR RESIDUE U2F A1477
source : AC1

8) chain A
residue 347
type
sequence A
description BINDING SITE FOR RESIDUE U2F A1477
source : AC1

9) chain A
residue 349
type
sequence Q
description BINDING SITE FOR RESIDUE U2F A1477
source : AC1

10) chain A
residue 364
type
sequence H
description BINDING SITE FOR RESIDUE U2F A1477
source : AC1

11) chain A
residue 366
type
sequence G
description BINDING SITE FOR RESIDUE U2F A1477
source : AC1

12) chain A
residue 367
type
sequence W
description BINDING SITE FOR RESIDUE U2F A1477
source : AC1

13) chain A
residue 368
type
sequence N
description BINDING SITE FOR RESIDUE U2F A1477
source : AC1

14) chain A
residue 369
type
sequence S
description BINDING SITE FOR RESIDUE U2F A1477
source : AC1

15) chain A
residue 372
type
sequence E
description BINDING SITE FOR RESIDUE U2F A1477
source : AC1

16) chain A
residue 386
type
sequence Y
description BINDING SITE FOR RESIDUE U2F A1477
source : AC1

17) chain A
residue 387
type
sequence A
description BINDING SITE FOR RESIDUE U2F A1477
source : AC1

18) chain A
residue 388
type
sequence E
description BINDING SITE FOR RESIDUE U2F A1477
source : AC1

19) chain A
residue 389
type
sequence Q
description BINDING SITE FOR RESIDUE U2F A1477
source : AC1

20) chain A
residue 19
type
sequence H
description BINDING SITE FOR RESIDUE TC7 A1478
source : AC2

21) chain A
residue 83
type
sequence E
description BINDING SITE FOR RESIDUE TC7 A1478
source : AC2

22) chain A
residue 118
type
sequence L
description BINDING SITE FOR RESIDUE TC7 A1478
source : AC2

23) chain A
residue 119
type
sequence F
description BINDING SITE FOR RESIDUE TC7 A1478
source : AC2

24) chain A
residue 183
type
sequence L
description BINDING SITE FOR RESIDUE TC7 A1478
source : AC2

25) chain A
residue 185
type
sequence P
description BINDING SITE FOR RESIDUE TC7 A1478
source : AC2

26) chain A
residue 315
type
sequence Y
description BINDING SITE FOR RESIDUE TC7 A1478
source : AC2

27) chain A
residue 387
type
sequence A
description BINDING SITE FOR RESIDUE TC7 A1478
source : AC2

28) chain A
residue 388
type
sequence E
description BINDING SITE FOR RESIDUE TC7 A1478
source : AC2

29) chain A
residue 275
type
sequence F
description BINDING SITE FOR RESIDUE EDO A1479
source : AC3

30) chain A
residue 280
type
sequence T
description BINDING SITE FOR RESIDUE EDO A1479
source : AC3

31) chain A
residue 281
type
sequence L
description BINDING SITE FOR RESIDUE EDO A1479
source : AC3

32) chain A
residue 286
type
sequence L
description BINDING SITE FOR RESIDUE EDO A1479
source : AC3

33) chain A
residue 302
type
sequence W
description BINDING SITE FOR RESIDUE EDO A1479
source : AC3

34) chain A
residue 303
type
sequence V
description BINDING SITE FOR RESIDUE EDO A1479
source : AC3

35) chain A
residue 304
type
sequence I
description BINDING SITE FOR RESIDUE EDO A1479
source : AC3

36) chain A
residue 305
type
sequence R
description BINDING SITE FOR RESIDUE EDO A1479
source : AC3

37) chain A
residue 117
type ACT_SITE
sequence D
description Charge relay => ECO:0000250|UniProtKB:A0A0A1HA03
source Swiss-Prot : SWS_FT_FI2

38) chain A
residue 277
type BINDING
sequence S
description BINDING => ECO:0000305|PubMed:18077347, ECO:0007744|PDB:2VCE
source Swiss-Prot : SWS_FT_FI3

39) chain A
residue 346
type BINDING
sequence W
description BINDING => ECO:0000305|PubMed:18077347, ECO:0007744|PDB:2VCE
source Swiss-Prot : SWS_FT_FI3

40) chain A
residue 347
type BINDING
sequence A
description BINDING => ECO:0000305|PubMed:18077347, ECO:0007744|PDB:2VCE
source Swiss-Prot : SWS_FT_FI3

41) chain A
residue 364
type BINDING
sequence H
description BINDING => ECO:0000305|PubMed:18077347, ECO:0007744|PDB:2VCE
source Swiss-Prot : SWS_FT_FI3

42) chain A
residue 367
type BINDING
sequence W
description BINDING => ECO:0000305|PubMed:18077347, ECO:0007744|PDB:2VCE
source Swiss-Prot : SWS_FT_FI3

43) chain A
residue 368
type BINDING
sequence N
description BINDING => ECO:0000305|PubMed:18077347, ECO:0007744|PDB:2VCE
source Swiss-Prot : SWS_FT_FI3

44) chain A
residue 369
type BINDING
sequence S
description BINDING => ECO:0000305|PubMed:18077347, ECO:0007744|PDB:2VCE
source Swiss-Prot : SWS_FT_FI3

45) chain A
residue 372
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:18077347, ECO:0007744|PDB:2VCE
source Swiss-Prot : SWS_FT_FI3

46) chain A
residue 386
type BINDING
sequence Y
description BINDING => ECO:0000305|PubMed:18077347, ECO:0007744|PDB:2VCE
source Swiss-Prot : SWS_FT_FI3

47) chain A
residue 388
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:18077347, ECO:0007744|PDB:2VCE
source Swiss-Prot : SWS_FT_FI3

48) chain A
residue 389
type BINDING
sequence Q
description BINDING => ECO:0000305|PubMed:18077347, ECO:0007744|PDB:2VCE
source Swiss-Prot : SWS_FT_FI3

49) chain A
residue 19
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000250|UniProtKB:A0A0A1HA03
source Swiss-Prot : SWS_FT_FI1

50) chain A
residue 346-389
type prosite
sequence WAPQAQVLAHPSTGGFLTHCGWNSTLESVVSGIPLIAWPL
YAEQ
description UDPGT UDP-glycosyltransferases signature. WapQaqVLahpstgGFLTHCGwnStleSVvsgi.PLiawPlyaEQ
source prosite : PS00375


Display surface

Download
Links