eF-site ID 5pzt-H
PDB Code 5pzt
Chain H

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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-(3-ethyl-4-phenylphenyl)sulfonylurea
Classification HYDROLASE/HYDROLASE INHIBITOR
Compound Fructose-1,6-bisphosphatase 1
Source (Q2TU34_HUMAN)
Sequence H:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV
RKAGIAKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIV
EPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTD
EPSEKDALQPGRNLVAAGYALYGSATMLVLAMDCGVNCFM
LDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKDFDPAVTE
YIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFLYP
ANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDV
IPTDIHQRAPVILGSPDDVLEFLKVYEKHS
Description


Functional site

1) chain H
residue 17
type
sequence V
description binding site for residue 947 H 401
source : AC8

2) chain H
residue 20
type
sequence E
description binding site for residue 947 H 401
source : AC8

3) chain H
residue 21
type
sequence G
description binding site for residue 947 H 401
source : AC8

4) chain H
residue 22
type
sequence R
description binding site for residue 947 H 401
source : AC8

5) chain H
residue 26
type
sequence G
description binding site for residue 947 H 401
source : AC8

6) chain H
residue 27
type
sequence T
description binding site for residue 947 H 401
source : AC8

7) chain H
residue 28
type
sequence G
description binding site for residue 947 H 401
source : AC8

8) chain H
residue 29
type
sequence E
description binding site for residue 947 H 401
source : AC8

9) chain H
residue 30
type
sequence L
description binding site for residue 947 H 401
source : AC8

10) chain H
residue 31
type
sequence T
description binding site for residue 947 H 401
source : AC8

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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


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