eF-site ID 5gk6-AB
PDB Code 5gk6
Chain A, B

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Title Structure of E.Coli fructose 1,6-bisphosphate aldolase, Citrate bound form
Classification LYASE
Compound Fructose-bisphosphate aldolase class 2
Source Escherichia coli (strain K12) (ALF_ECOLI)
Sequence A:  SKIFDFVKPGVITGDDVQKVFQVAKENNFALPAVNCVGTD
SINAVLETAAKVKAPVIVQFSNGGASFIAGKGVKSDVPQG
AAILGAISGAHHVHQMAEHYGVPVILHTDHCAKKLLPWID
GLLDAGEKHFAATGKPLFSSHMIDLSEESLQENIEICSKY
LERMSKIGMTLEIELGCTLYTQPEDVDYAYTELSKISPRF
TIAASFGNVVLTPTILRDSQEYVSKKHNLPHNSLNFVFHG
GSGSTAQEIKDSVSYGVVKMNIDTDTQWATWEGVLNYYKA
NEAYLQGQLGNPKGEDQPNKKYYDPRVWLRAGQTSMIARL
EKAFQELNAIDVL
B:  SKIFDFVKPGVITGDDVQKVFQVAKENNFALPAVNCVGTD
SINAVLETAAKVKAPVIVQFSNGGASFIAGKGVKSDVPQG
AAILGAISGAHHVHQMAEHYGVPVILHTDHCAKKLLPWID
GLLDAGEKHFAATGKPLFSSHMIDLSEESLQENIEICSKY
LERMSKIGMTLEIELGCLYTQPEDVDYAYTELSKISPRFT
IAASFGNVLTPTILRDSQEYVSKKHNLPHNSLNFVFHGGS
GSTAQEIKDSVSYGVVKMNIDTDTQWATWEGVLNYYKANE
AYLQGQLGNPKGEDQPNKKYYDPRVWLRAGQTSMIARLEK
AFQELNAIDVL
Description


Functional site

1) chain A
residue 110
type
sequence H
description binding site for residue ZN A 401
source : AC1

2) chain A
residue 264
type
sequence H
description binding site for residue ZN A 401
source : AC1

3) chain A
residue 110
type
sequence H
description binding site for residue CIT A 402
source : AC2

4) chain A
residue 264
type
sequence H
description binding site for residue CIT A 402
source : AC2

5) chain A
residue 265
type
sequence G
description binding site for residue CIT A 402
source : AC2

6) chain A
residue 88
type
sequence S
description binding site for residue PEG A 403
source : AC3

7) chain A
residue 91
type
sequence H
description binding site for residue PEG A 403
source : AC3

8) chain A
residue 92
type
sequence H
description binding site for residue PEG A 403
source : AC3

9) chain B
residue 88
type
sequence S
description binding site for residue PEG A 403
source : AC3

10) chain B
residue 91
type
sequence H
description binding site for residue PEG A 403
source : AC3

11) chain B
residue 92
type
sequence H
description binding site for residue PEG A 403
source : AC3

12) chain B
residue 95
type
sequence Q
description binding site for residue PEG A 403
source : AC3

13) chain B
residue 110
type
sequence H
description binding site for residue ZN B 401
source : AC4

14) chain B
residue 264
type
sequence H
description binding site for residue ZN B 401
source : AC4

15) chain B
residue 110
type
sequence H
description binding site for residue CIT B 402
source : AC5

16) chain B
residue 264
type
sequence H
description binding site for residue CIT B 402
source : AC5

17) chain B
residue 265
type
sequence G
description binding site for residue CIT B 402
source : AC5

18) chain A
residue 109
type catalytic
sequence D
description 52
source MCSA : MCSA1

19) chain A
residue 110
type catalytic
sequence H
description 52
source MCSA : MCSA1

20) chain A
residue 264
type catalytic
sequence H
description 52
source MCSA : MCSA1

21) chain A
residue 286
type catalytic
sequence N
description 52
source MCSA : MCSA1

22) chain B
residue 109
type catalytic
sequence D
description 52
source MCSA : MCSA2

23) chain B
residue 110
type catalytic
sequence H
description 52
source MCSA : MCSA2

24) chain B
residue 264
type catalytic
sequence H
description 52
source MCSA : MCSA2

25) chain B
residue 286
type catalytic
sequence N
description 52
source MCSA : MCSA2

26) chain A
residue 100-111
type prosite
sequence YGVPVILHTDHC
description ALDOLASE_CLASS_II_1 Fructose-bisphosphate aldolase class-II signature 1. Yg..VPVi.LHtDHC
source prosite : PS00602

27) chain A
residue 109
type ACT_SITE
sequence D
description Proton donor => ECO:0000269|PubMed:10080900
source Swiss-Prot : SWS_FT_FI1

28) chain B
residue 109
type ACT_SITE
sequence D
description Proton donor => ECO:0000269|PubMed:10080900
source Swiss-Prot : SWS_FT_FI1

29) chain A
residue 61
type BINDING
sequence S
description BINDING => ECO:0000305
source Swiss-Prot : SWS_FT_FI2

30) chain B
residue 61
type BINDING
sequence S
description BINDING => ECO:0000305
source Swiss-Prot : SWS_FT_FI2

31) chain A
residue 110
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10080900, ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754
source Swiss-Prot : SWS_FT_FI3

32) chain B
residue 264
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10080900, ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754
source Swiss-Prot : SWS_FT_FI3

33) chain A
residue 144
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:10080900, ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754
source Swiss-Prot : SWS_FT_FI3

34) chain A
residue 174
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10080900, ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754
source Swiss-Prot : SWS_FT_FI3

35) chain A
residue 264
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10080900, ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754
source Swiss-Prot : SWS_FT_FI3

36) chain B
residue 110
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10080900, ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754
source Swiss-Prot : SWS_FT_FI3

37) chain B
residue 144
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:10080900, ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754
source Swiss-Prot : SWS_FT_FI3

38) chain B
residue 174
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10080900, ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754
source Swiss-Prot : SWS_FT_FI3

39) chain A
residue 265
type BINDING
sequence G
description
source Swiss-Prot : SWS_FT_FI4

40) chain A
residue 286
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI4

41) chain B
residue 265
type BINDING
sequence G
description
source Swiss-Prot : SWS_FT_FI4

42) chain B
residue 286
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI4

43) chain A
residue 8
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122
source Swiss-Prot : SWS_FT_FI5

44) chain B
residue 8
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122
source Swiss-Prot : SWS_FT_FI5

45) chain A
residue 71
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000269|PubMed:21151122
source Swiss-Prot : SWS_FT_FI6

46) chain B
residue 250
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000269|PubMed:21151122
source Swiss-Prot : SWS_FT_FI6

47) chain B
residue 318
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000269|PubMed:21151122
source Swiss-Prot : SWS_FT_FI6

48) chain B
residue 325
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000269|PubMed:21151122
source Swiss-Prot : SWS_FT_FI6

49) chain B
residue 347
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000269|PubMed:21151122
source Swiss-Prot : SWS_FT_FI6

50) chain A
residue 114
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000269|PubMed:21151122
source Swiss-Prot : SWS_FT_FI6

51) chain A
residue 250
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000269|PubMed:21151122
source Swiss-Prot : SWS_FT_FI6

52) chain A
residue 318
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000269|PubMed:21151122
source Swiss-Prot : SWS_FT_FI6

53) chain A
residue 325
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000269|PubMed:21151122
source Swiss-Prot : SWS_FT_FI6

54) chain A
residue 347
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000269|PubMed:21151122
source Swiss-Prot : SWS_FT_FI6

55) chain B
residue 71
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000269|PubMed:21151122
source Swiss-Prot : SWS_FT_FI6

56) chain B
residue 114
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000269|PubMed:21151122
source Swiss-Prot : SWS_FT_FI6


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