eF-site ID 3t2c-A
PDB Code 3t2c
Chain A

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Title Fructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus neutrophilus, DHAP-bound form
Classification LYASE, HYDROLASE
Compound Fructose-1,6-bisphosphate aldolase/phosphatase
Source Thermoproteus neutrophilus (strain DSM 2338 / JCM 9278 / V24Sta) (B1YAL1_THENV)
Sequence A:  MRVTVSIIKADVGGFPGHAHVHPKMLEYAAAKLKEAQKRG
VIIDYFVYNVGDDISLLMTHTKGEDNKDIHGLAWETFKEV
TDQIAKRFKLYGAGQDLLKDAFSGNIRGMGPQVAEMEFEE
RPSEPIIAFAADKTEPGAFNLPLYKMFADPFTTAGLVIDP
SMHEGFIFEVLDVVEHKVYLLKTPEDAYSLLGLIGTTGRY
IIRKVFRRADGAPAAANSVERLSLIAGRYVGKDDPVLLVR
AQSGLPAVGEVLEAFAHPHLVHGWMRGSHAGPLMPARFIS
VDPERRIAIGPKMTRFDGPPKVGALGFQLHEGYLEGGVDL
FDDPAFDYVRQTAAQIADYIRRMGPFQPHRLPPEEMEYTA
LPKILAKVKPYPADQYEKDRKKYIEAVVK
Description


Functional site

1) chain A
residue 232
type
sequence K
description BINDING SITE FOR RESIDUE MG A 408
source : AC1

2) chain A
residue 234
type
sequence D
description BINDING SITE FOR RESIDUE MG A 408
source : AC1

3) chain A
residue 52
type
sequence D
description BINDING SITE FOR RESIDUE MG A 409
source : AC2

4) chain A
residue 53
type
sequence D
description BINDING SITE FOR RESIDUE MG A 409
source : AC2

5) chain A
residue 132
type
sequence D
description BINDING SITE FOR RESIDUE MG A 409
source : AC2

6) chain A
residue 133
type
sequence K
description BINDING SITE FOR RESIDUE MG A 409
source : AC2

7) chain A
residue 234
type
sequence D
description BINDING SITE FOR RESIDUE MG A 409
source : AC2

8) chain A
residue 11
type
sequence D
description BINDING SITE FOR RESIDUE MG A 410
source : AC3

9) chain A
residue 18
type
sequence H
description BINDING SITE FOR RESIDUE MG A 410
source : AC3

10) chain A
residue 52
type
sequence D
description BINDING SITE FOR RESIDUE MG A 410
source : AC3

11) chain A
residue 95
type
sequence Q
description BINDING SITE FOR RESIDUE MG A 410
source : AC3

12) chain A
residue 11
type
sequence D
description BINDING SITE FOR RESIDUE 13P A 411
source : AC4

13) chain A
residue 18
type
sequence H
description BINDING SITE FOR RESIDUE 13P A 411
source : AC4

14) chain A
residue 52
type
sequence D
description BINDING SITE FOR RESIDUE 13P A 411
source : AC4

15) chain A
residue 95
type
sequence Q
description BINDING SITE FOR RESIDUE 13P A 411
source : AC4

16) chain A
residue 132
type
sequence D
description BINDING SITE FOR RESIDUE 13P A 411
source : AC4

17) chain A
residue 133
type
sequence K
description BINDING SITE FOR RESIDUE 13P A 411
source : AC4

18) chain A
residue 229
type
sequence Y
description BINDING SITE FOR RESIDUE 13P A 411
source : AC4

19) chain A
residue 231
type
sequence G
description BINDING SITE FOR RESIDUE 13P A 411
source : AC4

20) chain A
residue 232
type
sequence K
description BINDING SITE FOR RESIDUE 13P A 411
source : AC4

21) chain A
residue 234
type
sequence D
description BINDING SITE FOR RESIDUE 13P A 411
source : AC4

22) chain A
residue 264
type
sequence W
description BINDING SITE FOR RESIDUE 13P A 411
source : AC4

23) chain A
residue 265
type
sequence M
description BINDING SITE FOR RESIDUE 13P A 411
source : AC4

24) chain A
residue 266
type
sequence R
description BINDING SITE FOR RESIDUE 13P A 411
source : AC4

25) chain A
residue 267
type
sequence G
description BINDING SITE FOR RESIDUE 13P A 411
source : AC4

26) chain A
residue 297
type
sequence D
description BINDING SITE FOR RESIDUE 13P A 411
source : AC4

27) chain A
residue 18
type
sequence H
description BINDING SITE FOR RESIDUE 13P A 412
source : AC5

28) chain A
residue 91
type
sequence Y
description BINDING SITE FOR RESIDUE 13P A 412
source : AC5

29) chain A
residue 229
type
sequence Y
description BINDING SITE FOR RESIDUE 13P A 412
source : AC5

30) chain A
residue 232
type
sequence K
description BINDING SITE FOR RESIDUE 13P A 412
source : AC5

31) chain A
residue 242
type
sequence Q
description BINDING SITE FOR RESIDUE 13P A 412
source : AC5

32) chain A
residue 243
type
sequence S
description BINDING SITE FOR RESIDUE 13P A 412
source : AC5

33) chain A
residue 247
type
sequence A
description BINDING SITE FOR RESIDUE 13P A 412
source : AC5

34) chain A
residue 266
type
sequence R
description BINDING SITE FOR RESIDUE 13P A 412
source : AC5

35) chain A
residue 297
type
sequence D
description BINDING SITE FOR RESIDUE 13P A 412
source : AC5

36) chain A
residue 358
type
sequence Y
description BINDING SITE FOR RESIDUE 13P A 412
source : AC5

37) chain A
residue 11
type ACT_SITE
sequence D
description Proton acceptor; for FBP phosphatase activity => ECO:0000250|UniProtKB:F9VMT6
source Swiss-Prot : SWS_FT_FI1

38) chain A
residue 229
type ACT_SITE
sequence Y
description Proton donor/acceptor; for FBP aldolase activity => ECO:0000305|PubMed:21983965
source Swiss-Prot : SWS_FT_FI2

39) chain A
residue 232
type ACT_SITE
sequence K
description Schiff-base intermediate with DHAP; for FBP aldolase activity => ECO:0000269|PubMed:21983965
source Swiss-Prot : SWS_FT_FI3

40) chain A
residue 11
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:21983965, ECO:0007744|PDB:3T2B, ECO:0007744|PDB:3T2C, ECO:0007744|PDB:3T2D
source Swiss-Prot : SWS_FT_FI4

41) chain A
residue 18
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:21983965, ECO:0007744|PDB:3T2B, ECO:0007744|PDB:3T2C, ECO:0007744|PDB:3T2D
source Swiss-Prot : SWS_FT_FI4

42) chain A
residue 52
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:21983965, ECO:0007744|PDB:3T2B, ECO:0007744|PDB:3T2C, ECO:0007744|PDB:3T2D
source Swiss-Prot : SWS_FT_FI4

43) chain A
residue 53
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:21983965, ECO:0007744|PDB:3T2B, ECO:0007744|PDB:3T2C, ECO:0007744|PDB:3T2D
source Swiss-Prot : SWS_FT_FI4

44) chain A
residue 132
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:21983965, ECO:0007744|PDB:3T2B, ECO:0007744|PDB:3T2C, ECO:0007744|PDB:3T2D
source Swiss-Prot : SWS_FT_FI4

45) chain A
residue 91
type BINDING
sequence Y
description in other chain => ECO:0000269|PubMed:21983965, ECO:0007744|PDB:3T2D
source Swiss-Prot : SWS_FT_FI5

46) chain A
residue 104
type BINDING
sequence G
description in other chain => ECO:0000269|PubMed:21983965, ECO:0007744|PDB:3T2D
source Swiss-Prot : SWS_FT_FI5

47) chain A
residue 358
type BINDING
sequence Y
description in other chain => ECO:0000269|PubMed:21983965, ECO:0007744|PDB:3T2D
source Swiss-Prot : SWS_FT_FI5

48) chain A
residue 95
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:21983965, ECO:0007744|PDB:3T2C, ECO:0007744|PDB:3T2D, ECO:0007744|PDB:3T2E
source Swiss-Prot : SWS_FT_FI6

49) chain A
residue 133
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:21983965, ECO:0007744|PDB:3T2C
source Swiss-Prot : SWS_FT_FI7

50) chain A
residue 266
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:21983965, ECO:0007744|PDB:3T2C
source Swiss-Prot : SWS_FT_FI7

51) chain A
residue 297
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:21983965, ECO:0007744|PDB:3T2C
source Swiss-Prot : SWS_FT_FI7

52) chain A
residue 232
type BINDING
sequence K
description BINDING => ECO:0000250|UniProtKB:F9VMT6
source Swiss-Prot : SWS_FT_FI8

53) chain A
residue 233
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:21983965
source Swiss-Prot : SWS_FT_FI9

54) chain A
residue 234
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:21983965
source Swiss-Prot : SWS_FT_FI9

55) chain A
residue 242
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:21983965
source Swiss-Prot : SWS_FT_FI9


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