eF-site ID 3tf4-AB
PDB Code 3tf4
Chain A, B

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Title ENDO/EXOCELLULASE:CELLOTRIOSE FROM THERMOMONOSPORA
Classification GLYCOSYL HYDROLASE
Compound T. FUSCA ENDO/EXO-CELLULASE E4 CATALYTIC DOMAIN AND CELLULOSE-BINDING DOMAIN
Source Thermomonospora fusca (GUN4_THEFU)
Sequence A:  EPAFNYAEALQKSMFFYEAQRSGKLPENNRVSWRGDSGLN
DGADVGLDLTGGWYDAGDHVKFGFPMAFTATMLAWGAIES
PEGYIRSGQMPYLKDNLRWVNDYFIKAHPSPNVLYVQVGD
GDADHKWWGPAEVMPMERPSFKVDPSCPGSDVAAETAAAM
AASSIVFADDDPAYAATLVQHAKQLYTFADTYRGVYSDCV
PAGAFYNSWSGYQDELVWGAYWLYKATGDDSYLAKAEYEY
DFLSTEQQTDLRSYRWTIAWDDKSYGTYVLLAKETGKQKY
IDDANRWLDYWTVGVNGQRVPYSPGGMAVLDTWGALRYAA
NTAFVALVYAKVIDDPVRKQRYHDFAVRQINYALGDNPRN
SSYVVGFGNNPPRNPHHRTAHGSWTDSIASPAENRHVLYG
ALVGGPGSPNDAYTDDRQDYVANEVATDYNAGFSSALAML
VEEYGGTPLADFPPTEEPDGPEIFVEAQINTPGTTFTEIK
AMIRNQSGWPARMLDKGTFRYWFTLDEGVDPADITVSSAY
NQCATPEDVHHVSGDLYYVEIDCTGEKIFPGGQSEHRREV
QFRIAGGPGWDPSNDWSFQGIGNELAPAPYIVLYDDGVPV
WGTAP
B:  EPAFNYAEALQKSMFFYEAQRSGKLPENNRVSWRGDSGLN
DGADVGLDLTGGWYDAGDHVKFGFPMAFTATMLAWGAIES
PEGYIRSGQMPYLKDNLRWVNDYFIKAHPSPNVLYVQVGD
GDADHKWWGPAEVMPMERPSFKVDPSCPGSDVAAETAAAM
AASSIVFADDDPAYAATLVQHAKQLYTFADTYRGVYSDCV
PAGAFYNSWSGYQDELVWGAYWLYKATGDDSYLAKAEYEY
DFLSTEQQTDLRSYRWTIAWDDKSYGTYVLLAKETGKQKY
IDDANRWLDYWTVGVNGQRVPYSPGGMAVLDTWGALRYAA
NTAFVALVYAKVIDDPVRKQRYHDFAVRQINYALGDNPRN
SSYVVGFGNNPPRNPHHRTAHGSWTDSIASPAENRHVLYG
ALVGGPGSPNDAYTDDRQDYVANEVATDYNAGFSSALAML
VEEYGGTPLADFPPTEEPDGPEIFVEAQINTPGTTFTEIK
AMIRNQSGWPARMLDKGTFRYWFTLDEGVDPADITVSSAY
NQCATPEDVHHVSGDLYYVEIDCTGEKIFPGGQSEHRREV
QFRIAGGPGWDPSNDWSFQGIGNELAPAPYIVLYDDGVPV
WGTAP
Description (1)  T. FUSCA ENDO/EXO-CELLULASE E4 CATALYTIC DOMAIN AND CELLULOSE-BINDING DOMAIN


Functional site

1) chain A
residue 210
type
sequence S
description CA BINDING SITE.
source : CA1

2) chain A
residue 211
type
sequence G
description CA BINDING SITE.
source : CA1

3) chain A
residue 214
type
sequence D
description CA BINDING SITE.
source : CA1

4) chain A
residue 215
type
sequence E
description CA BINDING SITE.
source : CA1

5) chain A
residue 261
type
sequence D
description CA BINDING SITE.
source : CA1

6) chain B
residue 210
type
sequence S
description CA BINDING SITE.
source : CA2

7) chain B
residue 211
type
sequence G
description CA BINDING SITE.
source : CA2

8) chain B
residue 214
type
sequence D
description CA BINDING SITE.
source : CA2

9) chain B
residue 215
type
sequence E
description CA BINDING SITE.
source : CA2

10) chain B
residue 261
type
sequence D
description CA BINDING SITE.
source : CA2

11) chain A
residue 504
type
sequence T
description CA BINDING SITE.
source : CA3

12) chain A
residue 506
type
sequence D
description CA BINDING SITE.
source : CA3

13) chain A
residue 571
type
sequence D
description CA BINDING SITE.
source : CA3

14) chain A
residue 574
type
sequence N
description CA BINDING SITE.
source : CA3

15) chain A
residue 575
type
sequence D
description CA BINDING SITE.
source : CA3

16) chain B
residue 504
type
sequence T
description CA BINDING SITE.
source : CA4

17) chain B
residue 506
type
sequence D
description CA BINDING SITE.
source : CA4

18) chain B
residue 571
type
sequence D
description CA BINDING SITE.
source : CA4

19) chain B
residue 574
type
sequence N
description CA BINDING SITE.
source : CA4

20) chain B
residue 575
type
sequence D
description CA BINDING SITE.
source : CA4

21) chain A
residue 55
type
sequence D
description ACTIVE SITE.
source : AA1

22) chain A
residue 58
type
sequence D
description ACTIVE SITE.
source : AA1

23) chain A
residue 424
type
sequence E
description ACTIVE SITE.
source : AA1

24) chain B
residue 55
type
sequence D
description ACTIVE SITE.
source : AB1

25) chain B
residue 58
type
sequence D
description ACTIVE SITE.
source : AB1

26) chain B
residue 424
type
sequence E
description ACTIVE SITE.
source : AB1

27) chain A
residue 55
type catalytic
sequence D
description 559
source MCSA : MCSA1

28) chain A
residue 58
type catalytic
sequence D
description 559
source MCSA : MCSA1

29) chain A
residue 206
type catalytic
sequence Y
description 559
source MCSA : MCSA1

30) chain A
residue 424
type catalytic
sequence E
description 559
source MCSA : MCSA1

31) chain B
residue 55
type catalytic
sequence D
description 559
source MCSA : MCSA2

32) chain B
residue 58
type catalytic
sequence D
description 559
source MCSA : MCSA2

33) chain B
residue 206
type catalytic
sequence Y
description 559
source MCSA : MCSA2

34) chain B
residue 424
type catalytic
sequence E
description 559
source MCSA : MCSA2

35) chain A
residue 58
type ACT_SITE
sequence D
description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10140
source Swiss-Prot : SWS_FT_FI1

36) chain B
residue 58
type ACT_SITE
sequence D
description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10140
source Swiss-Prot : SWS_FT_FI1

37) chain A
residue 376
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10059
source Swiss-Prot : SWS_FT_FI2

38) chain B
residue 376
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10059
source Swiss-Prot : SWS_FT_FI2

39) chain A
residue 381
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

40) chain B
residue 381
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

41) chain A
residue 415
type ACT_SITE
sequence D
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10060
source Swiss-Prot : SWS_FT_FI4

42) chain A
residue 424
type ACT_SITE
sequence E
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10060
source Swiss-Prot : SWS_FT_FI4

43) chain B
residue 415
type ACT_SITE
sequence D
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10060
source Swiss-Prot : SWS_FT_FI4

44) chain B
residue 424
type ACT_SITE
sequence E
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10060
source Swiss-Prot : SWS_FT_FI4

45) chain A
residue 352-378
type prosite
sequence YALGDNPRNSSYVVGFGNNPPRNPHHR
description GH9_2 Glycosyl hydrolases family 9 (GH9) active site signature 2. YALGdNprnsSYVVGf....GnnPPrnPHHR
source prosite : PS00592

46) chain A
residue 413-431
type prosite
sequence YTDDRQDYVANEVATDYNA
description GH9_3 Glycosyl hydrolases family 9 (GH9) active site signature 3. YtDdrqdYvanEvAtdyNA
source prosite : PS00698

47) chain A
residue 49-66
type prosite
sequence LTGGWYDAGDHVKFGFPM
description GH9_1 Glycosyl hydrolases family 9 (GH9) active site signature 1. LtGGWYDAGDhvKFgFPM
source prosite : PS60032


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