eF-site ID 5q01-E
PDB Code 5q01
Chain E

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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-(5-bromo-1,3-thiazol-2-yl)-3-[4-(4,5-dichloro-2-methylpyrazol-3-yl)oxyphenyl]sulfonylurea
Classification HYDROLASE/HYDROLASE INHIBITOR
Compound Fructose-1,6-bisphosphatase 1
Source (Q2TU34_HUMAN)
Sequence E:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV
RKAGIAHLYGIAGVKKLDVLSNDLVMNMLKSSFATCVLVS
EEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIF
GIYRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLA
MDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYA
KDFDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTL
VYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMAT
TGKEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS
Description


Functional site

1) chain E
residue 21
type
sequence G
description binding site for residue 95G E 401
source : AC5

2) chain E
residue 24
type
sequence A
description binding site for residue 95G E 401
source : AC5

3) chain E
residue 26
type
sequence G
description binding site for residue 95G E 401
source : AC5

4) chain E
residue 27
type
sequence T
description binding site for residue 95G E 401
source : AC5

5) chain E
residue 28
type
sequence G
description binding site for residue 95G E 401
source : AC5

6) chain E
residue 29
type
sequence E
description binding site for residue 95G E 401
source : AC5

7) chain E
residue 30
type
sequence L
description binding site for residue 95G E 401
source : AC5

8) chain E
residue 31
type
sequence T
description binding site for residue 95G E 401
source : AC5

9) chain E
residue 34
type
sequence L
description binding site for residue 95G E 401
source : AC5

10) chain E
residue 161
type
sequence A
description binding site for residue 95G E 401
source : AC5

11) chain E
residue 175
type
sequence L
description binding site for residue 95G E 401
source : AC5

12) chain E
residue 177
type
sequence M
description binding site for residue 95G E 401
source : AC5

13) chain E
residue 27
type
sequence T
description binding site for residue 95G G 401
source : AC7

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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


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