eF-site ID 5pzw-A
PDB Code 5pzw
Chain A

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Title Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed with the allosteric inhibitor 1-(3-chlorophenyl)sulfonyl-3-[5-[(3-chlorophenyl)sulfonylcarbamoylamino]pentyl]urea
Classification HYDROLASE/HYDROLASE inhibitor
Compound Fructose-1,6-bisphosphatase 1
Source (Q2TU34_HUMAN)
Sequence A:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV
RKAGIAHLYGIAGVKKLDVLSNDLVMNMLKSSFATCVLVS
EEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIF
GIYRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLA
MDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYA
KDFDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTL
VYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMAT
TGKEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS
Description


Functional site

1) chain A
residue 17
type
sequence V
description binding site for residue 94J A 401
source : AC1

2) chain A
residue 18
type
sequence M
description binding site for residue 94J A 401
source : AC1

3) chain A
residue 21
type
sequence G
description binding site for residue 94J A 401
source : AC1

4) chain A
residue 24
type
sequence A
description binding site for residue 94J A 401
source : AC1

5) chain A
residue 26
type
sequence G
description binding site for residue 94J A 401
source : AC1

6) chain A
residue 27
type
sequence T
description binding site for residue 94J A 401
source : AC1

7) chain A
residue 28
type
sequence G
description binding site for residue 94J A 401
source : AC1

8) chain A
residue 29
type
sequence E
description binding site for residue 94J A 401
source : AC1

9) chain A
residue 30
type
sequence L
description binding site for residue 94J A 401
source : AC1

10) chain A
residue 31
type
sequence T
description binding site for residue 94J A 401
source : AC1

11) chain A
residue 17
type
sequence V
description binding site for residue AMZ A 402
source : AC2

12) chain A
residue 20
type
sequence E
description binding site for residue AMZ A 402
source : AC2

13) chain A
residue 27
type
sequence T
description binding site for residue AMZ A 402
source : AC2

14) chain A
residue 29
type
sequence E
description binding site for residue AMZ A 402
source : AC2

15) chain A
residue 30
type
sequence L
description binding site for residue AMZ A 402
source : AC2

16) chain A
residue 31
type
sequence T
description binding site for residue AMZ A 402
source : AC2

17) chain A
residue 112
type
sequence K
description binding site for residue AMZ A 402
source : AC2

18) chain A
residue 113
type
sequence Y
description binding site for residue AMZ A 402
source : AC2

19) chain A
residue 140
type
sequence R
description binding site for residue AMZ A 402
source : AC2

20) chain A
residue 17
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

21) chain A
residue 27
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

22) chain A
residue 112
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

23) chain A
residue 140
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

24) chain A
residue 97
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

25) chain A
residue 120
type BINDING
sequence L
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

26) chain A
residue 212
type BINDING
sequence N
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

27) chain A
residue 243
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

28) chain A
residue 264
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

29) chain A
residue 274
type BINDING
sequence K
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

30) chain A
residue 118
type BINDING
sequence D
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

31) chain A
residue 121
type BINDING
sequence D
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

32) chain A
residue 280
type BINDING
sequence E
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

33) chain A
residue 215
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI6

34) chain A
residue 244
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI6

35) chain A
residue 264
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI7

36) chain A
residue 273-285
type prosite
sequence GKLRLLYECNPMA
description FBPASE Fructose-1-6-bisphosphatase active site. GKLrlLYEcnPMA
source prosite : PS00124

37) chain A
residue 150
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI5


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