eF-site ID 5pzu-C
PDB Code 5pzu
Chain C

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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 [5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
Classification HYDROLASE/HYDROLASE INHIBITOR
Compound Fructose-1,6-bisphosphatase 1
Source (Q2TU34_HUMAN)
Sequence C:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV
RKAGIAHLYGIAGKKLDVLSNDLVMNMLKSSFATCVLVSE
EDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFG
IYRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAM
DCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAK
DFDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLV
YGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATT
GKEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS
Description


Functional site

1) chain C
residue 17
type
sequence V
description binding site for residue 94D C 401
source : AC3

2) chain C
residue 20
type
sequence E
description binding site for residue 94D C 401
source : AC3

3) chain C
residue 21
type
sequence G
description binding site for residue 94D C 401
source : AC3

4) chain C
residue 26
type
sequence G
description binding site for residue 94D C 401
source : AC3

5) chain C
residue 27
type
sequence T
description binding site for residue 94D C 401
source : AC3

6) chain C
residue 28
type
sequence G
description binding site for residue 94D C 401
source : AC3

7) chain C
residue 29
type
sequence E
description binding site for residue 94D C 401
source : AC3

8) chain C
residue 30
type
sequence L
description binding site for residue 94D C 401
source : AC3

9) chain C
residue 31
type
sequence T
description binding site for residue 94D C 401
source : AC3

10) chain C
residue 112
type
sequence K
description binding site for residue 94D C 401
source : AC3

11) chain C
residue 113
type
sequence Y
description binding site for residue 94D C 401
source : AC3

12) chain C
residue 160
type
sequence V
description binding site for residue 94D C 401
source : AC3

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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


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