eF-site ID 2cet-AB
PDB Code 2cet
Chain A, B

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Title Beta-glucosidase from Thermotoga maritima in complex with phenethyl- substituted glucoimidazole
Classification HYDROLASE
Compound BETA-GLUCOSIDASE A
Source Thermotoga maritima (BGLA_THEMA)
Sequence A:  VKKFPEGFLWGVATASYQIEGSPLADGAGMSIWHTFSHTP
GNVKNGDTGDVACDHYNRWKEDIEIIEKLGVKAYRFSISW
PRILPEGTGRVNQKGLDFYNRIIDTLLEKGITPFVTIYHW
DLPFALQLKGGWANREIADWFAEYSRVLFENFGDRVKNWI
TLNEPWVVAIVGHLYGVHAPGMRDIYVAFRAVHNLLRAHA
RAVKVFRETVKDGKIGIVFNNGYFEPASERAVRFMHQFNN
YPLFLNPIYRGDYPELVLEFAREYLPENYKDDMSEIQEKI
DFVGLNYYSGHLVKFDPAKVSFVERDLPKTAMGWEIVPEG
IYWILKKVKEEYNPPEVYITENGAAFDDVVSEDGRVHDQN
RIDYLKAHIGQAWKAIQEGVPLKGYFVWSLLDNFEWAEGY
SKRFGIVYVDYSTQKRIVKDSGYWYSNVVKNNGLE
B:  NVKKFPEGFLWGVATASYQIEGSPLADGAGMSIWHTFSHT
PGNVKNGDTGDVACDHYNRWKEDIEIIEKLGVKAYRFSIS
WPRILPEGTGRVNQKGLDFYNRIIDTLLEKGITPFVTIYH
WDLPFALQLKGGWANREIADWFAEYSRVLFENFGDRVKNW
ITLNEPWVVAIVGHLYGVHAPGMRDIYVAFRAVHNLLRAH
ARAVKVFRETVKDGKIGIVFNNGYFEPASEKEEDIRAVRF
MHQFNNYPLFLNPIYRGDYPELVLEFAREYLPENYKDDMS
EIQEKIDFVGLNYYSGHLVKFDPDAKVSFVERDLPKTAMG
WEIVPEGIYWILKKVKEEYNPPEVYITENGAAFDDVVSED
GRVHDQNRIDYLKAHIGQAWKAIQEGVPLKGYFVWSLLDN
FEWAEGYSKRFGIVYVDYSTQKRIVKDSGYWYSNVVKNNG
LE
Description


Functional site

1) chain A
residue 54
type
sequence A
description BINDING SITE FOR RESIDUE ACT A1446
source : AC1

2) chain A
residue 421
type
sequence Y
description BINDING SITE FOR RESIDUE ACT A1446
source : AC1

3) chain B
residue 278
type
sequence D
description BINDING SITE FOR RESIDUE CA B1446
source : AC2

4) chain B
residue 281
type
sequence S
description BINDING SITE FOR RESIDUE CA B1446
source : AC2

5) chain B
residue 282
type
sequence E
description BINDING SITE FOR RESIDUE CA B1446
source : AC2

6) chain A
residue 20
type
sequence Q
description BINDING SITE FOR RESIDUE PGI A1447
source : AC3

7) chain A
residue 121
type
sequence H
description BINDING SITE FOR RESIDUE PGI A1447
source : AC3

8) chain A
residue 165
type
sequence N
description BINDING SITE FOR RESIDUE PGI A1447
source : AC3

9) chain A
residue 166
type
sequence E
description BINDING SITE FOR RESIDUE PGI A1447
source : AC3

10) chain A
residue 295
type
sequence Y
description BINDING SITE FOR RESIDUE PGI A1447
source : AC3

11) chain A
residue 324
type
sequence W
description BINDING SITE FOR RESIDUE PGI A1447
source : AC3

12) chain A
residue 351
type
sequence E
description BINDING SITE FOR RESIDUE PGI A1447
source : AC3

13) chain A
residue 398
type
sequence W
description BINDING SITE FOR RESIDUE PGI A1447
source : AC3

14) chain A
residue 405
type
sequence E
description BINDING SITE FOR RESIDUE PGI A1447
source : AC3

15) chain A
residue 406
type
sequence W
description BINDING SITE FOR RESIDUE PGI A1447
source : AC3

16) chain A
residue 414
type
sequence F
description BINDING SITE FOR RESIDUE PGI A1447
source : AC3

17) chain B
residue 20
type
sequence Q
description BINDING SITE FOR RESIDUE PGI B1447
source : AC4

18) chain B
residue 121
type
sequence H
description BINDING SITE FOR RESIDUE PGI B1447
source : AC4

19) chain B
residue 122
type
sequence W
description BINDING SITE FOR RESIDUE PGI B1447
source : AC4

20) chain B
residue 165
type
sequence N
description BINDING SITE FOR RESIDUE PGI B1447
source : AC4

21) chain B
residue 166
type
sequence E
description BINDING SITE FOR RESIDUE PGI B1447
source : AC4

22) chain B
residue 169
type
sequence V
description BINDING SITE FOR RESIDUE PGI B1447
source : AC4

23) chain B
residue 295
type
sequence Y
description BINDING SITE FOR RESIDUE PGI B1447
source : AC4

24) chain B
residue 324
type
sequence W
description BINDING SITE FOR RESIDUE PGI B1447
source : AC4

25) chain B
residue 351
type
sequence E
description BINDING SITE FOR RESIDUE PGI B1447
source : AC4

26) chain B
residue 398
type
sequence W
description BINDING SITE FOR RESIDUE PGI B1447
source : AC4

27) chain B
residue 405
type
sequence E
description BINDING SITE FOR RESIDUE PGI B1447
source : AC4

28) chain B
residue 406
type
sequence W
description BINDING SITE FOR RESIDUE PGI B1447
source : AC4

29) chain B
residue 414
type
sequence F
description BINDING SITE FOR RESIDUE PGI B1447
source : AC4

30) chain A
residue 166
type ACT_SITE
sequence E
description Proton donor => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

31) chain B
residue 166
type ACT_SITE
sequence E
description Proton donor => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

32) chain A
residue 351
type ACT_SITE
sequence E
description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055
source Swiss-Prot : SWS_FT_FI2

33) chain B
residue 351
type ACT_SITE
sequence E
description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055
source Swiss-Prot : SWS_FT_FI2

34) chain A
residue 347-355
type prosite
sequence VYITENGAA
description GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. VYITENGAA
source prosite : PS00572

35) chain A
residue 10-24
type prosite
sequence FLWGVATASYQIEGS
description GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlWGvAtASYQiEgS
source prosite : PS00653


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