eF-site ID 1fpg-B
PDB Code 1fpg
Chain B

click to enlarge
Title STRUCTURAL ASPECTS OF THE ALLOSTERIC INHIBITION OF FRUCTOSE-1,6-BISPHOSPHATASE BY AMP: THE BINDING OF BOTH THE SUBSTRATE ANALOGUE 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND CATALYTIC METAL IONS MONITORED BY X-RAY CRYSTALLOGRAPHY
Classification HYDROLASE (PHOSPHORIC MONOESTER)
Compound FRUCTOSE 1,6-BISPHOSPHATASE
Source null (F16P_PIG)
Sequence B:  NIVTLTRFVMEQGRKARGTGEMTQLLNSLCTAVKAISTAV
RKAGIAHLYGIAGKLDVLSNDLVINVLKSSFATCVLVTEE
DKNAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGI
YRKNSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMV
NGVNCFMLDPAIGEFILVDRNVKIKKKGSIYSINEGYAKE
FDPAITEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVY
GGIFMYPANKKSPKGKLRLLYECNPMAYVMEKAGGLATTG
KEAVLDIVPTDIHQRAPIILGSPEDVTELLEIYQKHA
Description (1)  FRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPHOHYDROLASE) (E.C.3.1.3.11) COMPLEXED WITH AMP, 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE, AND MN2+ (CONCENTRATION OF 300 MICROMOLAR)


Functional site
1) chain B
residue 20
type
sequence Q
description AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN B
source : AM2
2) chain B
residue 17
type
sequence V
description AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN B
source : AM2
3) chain B
residue 31
type
sequence T
description AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN B
source : AM2
4) chain B
residue 140
type
sequence R
description AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN B
source : AM2
5) chain B
residue 113
type
sequence Y
description AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN B
source : AM2
6) chain B
residue 29
type
sequence E
description AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN B
source : AM2
7) chain B
residue 30
type
sequence M
description AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN B
source : AM2
8) chain B
residue 27
type
sequence T
description AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN B
source : AM2
9) chain B
residue 112
type
sequence K
description AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN B
source : AM2
10) chain B
residue 177
type
sequence M
description AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN B
source : AM2
11) chain B
residue 24
type
sequence A
description AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN B
source : AM2
12) chain B
residue 21
type
sequence G
description AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN B
source : AM2
13) chain B
residue 26
type
sequence G
description AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN B
source : AM2
14) chain B
residue 243
type
sequence R
description ACTIVE SITE IN MONOMER COMPOSED OF CHAIN A
source : AC1
15) chain B
residue 244
type
sequence Y
description ACTIVE SITE IN MONOMER COMPOSED OF CHAIN B
source : AC2
16) chain B
residue 212
type
sequence N
description ACTIVE SITE IN MONOMER COMPOSED OF CHAIN B
source : AC2
17) chain B
residue 215
type
sequence Y
description ACTIVE SITE IN MONOMER COMPOSED OF CHAIN B
source : AC2
18) chain B
residue 264
type
sequence Y
description ACTIVE SITE IN MONOMER COMPOSED OF CHAIN B
source : AC2
19) chain B
residue 274
type
sequence K
description ACTIVE SITE IN MONOMER COMPOSED OF CHAIN B
source : AC2
20) chain B
residue 248
type
sequence M
description ACTIVE SITE IN MONOMER COMPOSED OF CHAIN B
source : AC2
21) chain B
residue 276
type
sequence R
description ACTIVE SITE IN MONOMER COMPOSED OF CHAIN B
source : AC2
22) chain B
residue 280
type
sequence E
description ACTIVE SITE IN MONOMER COMPOSED OF CHAIN B
source : AC2
23) chain B
residue 122
type
sequence G
description ACTIVE SITE IN MONOMER COMPOSED OF CHAIN B
source : AC2
24) chain B
residue 121
type
sequence D
description ACTIVE SITE IN MONOMER COMPOSED OF CHAIN B
source : AC2
25) chain B
residue 97
type
sequence E
description FIRST METAL SITE IN MONOMER COMPOSED OF CHAIN B
source : MA2
26) chain B
residue 118
type
sequence D
description FIRST METAL SITE IN MONOMER COMPOSED OF CHAIN B
source : MA2
27) chain B
residue 280
type
sequence E
description FIRST METAL SITE IN MONOMER COMPOSED OF CHAIN B
source : MA2
28) chain B
residue 121
type
sequence D
description FIRST METAL SITE IN MONOMER COMPOSED OF CHAIN B
source : MA2
29) chain B
residue 97
type
sequence E
description SECOND METAL SITE IN MONOMERS COMPOSED OF CHAIN B
source : MA4
30) chain B
residue 118
type
sequence D
description SECOND METAL SITE IN MONOMERS COMPOSED OF CHAIN B
source : MA4
31) chain B
residue 120
type
sequence L
description SECOND METAL SITE IN MONOMERS COMPOSED OF CHAIN B
source : MA4
32) chain B
residue 98
type
sequence E
description SECOND METAL SITE IN MONOMERS COMPOSED OF CHAIN B
source : MA4
33) chain B
residue 75
type catalytic
sequence V
description 546
source MCSA : MCSA2
34) chain B
residue 98
type catalytic
sequence E
description 546
source MCSA : MCSA2
35) chain B
residue 99
type catalytic
sequence D
description 546
source MCSA : MCSA2
36) chain B
residue 119
type catalytic
sequence P
description 546
source MCSA : MCSA2
37) chain B
residue 121
type catalytic
sequence D
description 546
source MCSA : MCSA2
38) chain B
residue 122
type catalytic
sequence G
description 546
source MCSA : MCSA2
39) chain B
residue 281
type catalytic
sequence C
description 546
source MCSA : MCSA2
40) chain B
residue 216
type MOD_RES
sequence A
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI10
41) chain B
residue 245
type MOD_RES
sequence V
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI10
42) chain B
residue 265
type MOD_RES
sequence P
description Phosphotyrosine => ECO:0000250|UniProtKB:P09467
source Swiss-Prot : SWS_FT_FI11
43) chain B
residue 119
type BINDING
sequence P
description BINDING => ECO:0000269|PubMed:2164670
source Swiss-Prot : SWS_FT_FI2
44) chain B
residue 121
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:2164670
source Swiss-Prot : SWS_FT_FI2
45) chain B
residue 122
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:2164670
source Swiss-Prot : SWS_FT_FI2
46) chain B
residue 141
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:2164670
source Swiss-Prot : SWS_FT_FI2
47) chain B
residue 281
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:2164670
source Swiss-Prot : SWS_FT_FI2
48) chain B
residue 98
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:2164670
source Swiss-Prot : SWS_FT_FI2
49) chain B
residue 18
type BINDING
sequence M
description BINDING => ECO:0000269|PubMed:10913263, ECO:0000269|PubMed:15767255, ECO:0000269|PubMed:2164670, ECO:0007744|PDB:1EYJ, ECO:0007744|PDB:1EYK, ECO:0007744|PDB:1FBP, ECO:0007744|PDB:1FJ9, ECO:0007744|PDB:1FPD, ECO:0007744|PDB:1FPE, ECO:0007744|PDB:1FPF, ECO:0007744|PDB:1FPG, ECO:0007744|PDB:1FPI, ECO:0007744|PDB:1FPJ, ECO:0007744|PDB:1FPL, ECO:0007744|PDB:1FRP, ECO:0007744|PDB:1FSA, ECO:0007744|PDB:1KZ8, ECO:0007744|PDB:1NV7, ECO:0007744|PDB:1RDY, ECO:0007744|PDB:1RDZ, ECO:0007744|PDB:1YYZ, ECO:0007744|PDB:1YZ0, ECO:0007744|PDB:2F3D, ECO:0007744|PDB:4FBP, ECO:0007744|PDB:4GBV, ECO:0007744|PDB:4GBW, ECO:0007744|PDB:4GWS, ECO:0007744|PDB:4GWY, ECO:0007744|PDB:4GWZ, ECO:0007744|PDB:4GX4, ECO:0007744|PDB:4GX6, ECO:0007744|PDB:4H46, ECO:0007744|PDB:4KXP
source Swiss-Prot : SWS_FT_FI1
50) chain B
residue 28
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:10913263, ECO:0000269|PubMed:15767255, ECO:0000269|PubMed:2164670, ECO:0007744|PDB:1EYJ, ECO:0007744|PDB:1EYK, ECO:0007744|PDB:1FBP, ECO:0007744|PDB:1FJ9, ECO:0007744|PDB:1FPD, ECO:0007744|PDB:1FPE, ECO:0007744|PDB:1FPF, ECO:0007744|PDB:1FPG, ECO:0007744|PDB:1FPI, ECO:0007744|PDB:1FPJ, ECO:0007744|PDB:1FPL, ECO:0007744|PDB:1FRP, ECO:0007744|PDB:1FSA, ECO:0007744|PDB:1KZ8, ECO:0007744|PDB:1NV7, ECO:0007744|PDB:1RDY, ECO:0007744|PDB:1RDZ, ECO:0007744|PDB:1YYZ, ECO:0007744|PDB:1YZ0, ECO:0007744|PDB:2F3D, ECO:0007744|PDB:4FBP, ECO:0007744|PDB:4GBV, ECO:0007744|PDB:4GBW, ECO:0007744|PDB:4GWS, ECO:0007744|PDB:4GWY, ECO:0007744|PDB:4GWZ, ECO:0007744|PDB:4GX4, ECO:0007744|PDB:4GX6, ECO:0007744|PDB:4H46, ECO:0007744|PDB:4KXP
source Swiss-Prot : SWS_FT_FI1
51) chain B
residue 113
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:10913263, ECO:0000269|PubMed:15767255, ECO:0000269|PubMed:2164670, ECO:0007744|PDB:1EYJ, ECO:0007744|PDB:1EYK, ECO:0007744|PDB:1FBP, ECO:0007744|PDB:1FJ9, ECO:0007744|PDB:1FPD, ECO:0007744|PDB:1FPE, ECO:0007744|PDB:1FPF, ECO:0007744|PDB:1FPG, ECO:0007744|PDB:1FPI, ECO:0007744|PDB:1FPJ, ECO:0007744|PDB:1FPL, ECO:0007744|PDB:1FRP, ECO:0007744|PDB:1FSA, ECO:0007744|PDB:1KZ8, ECO:0007744|PDB:1NV7, ECO:0007744|PDB:1RDY, ECO:0007744|PDB:1RDZ, ECO:0007744|PDB:1YYZ, ECO:0007744|PDB:1YZ0, ECO:0007744|PDB:2F3D, ECO:0007744|PDB:4FBP, ECO:0007744|PDB:4GBV, ECO:0007744|PDB:4GBW, ECO:0007744|PDB:4GWS, ECO:0007744|PDB:4GWY, ECO:0007744|PDB:4GWZ, ECO:0007744|PDB:4GX4, ECO:0007744|PDB:4GX6, ECO:0007744|PDB:4H46, ECO:0007744|PDB:4KXP
source Swiss-Prot : SWS_FT_FI1
52) chain B
residue 213
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10913263, ECO:0000269|PubMed:12595528, ECO:0000269|PubMed:1312721, ECO:0000269|PubMed:14530289, ECO:0000269|PubMed:15767255, ECO:0000269|PubMed:17933867, ECO:0000269|PubMed:1849642, ECO:0000269|PubMed:2157849, ECO:0000269|PubMed:2164670, ECO:0007744|PDB:1CNQ, ECO:0007744|PDB:1EYI, ECO:0007744|PDB:1EYJ, ECO:0007744|PDB:1EYK, ECO:0007744|PDB:1FBP, ECO:0007744|PDB:1FJ6, ECO:0007744|PDB:1FJ9, ECO:0007744|PDB:1FRP, ECO:0007744|PDB:1FSA, ECO:0007744|PDB:1KZ8, ECO:0007744|PDB:1LEV, ECO:0007744|PDB:1NUW, ECO:0007744|PDB:1NUX, ECO:0007744|PDB:1NUY, ECO:0007744|PDB:1NUZ, ECO:0007744|PDB:1NV0, ECO:0007744|PDB:1NV1, ECO:0007744|PDB:1NV2, ECO:0007744|PDB:1NV3, ECO:0007744|PDB:1NV4, ECO:0007744|PDB:1NV5, ECO:0007744|PDB:1NV6, ECO:0007744|PDB:1NV7, ECO:0007744|PDB:1Q9D, ECO:0007744|PDB:1RDY, ECO:0007744|PDB:1RDZ, ECO:0007744|PDB:1YXI, ECO:0007744|PDB:1YYZ, ECO:0007744|PDB:1YZ0, ECO:0007744|PDB:2F3B, ECO:0007744|PDB:2F3D, ECO:0007744|PDB:2QVU, ECO:0007744|PDB:2QVV, ECO:0007744|PDB:3FBP, ECO:0007744|PDB:4GBV, ECO:0007744|PDB:4GBW, ECO:0007744|PDB:4GWS, ECO:0007744|PDB:4GWU, ECO:0007744|PDB:4GWW, ECO:0007744|PDB:4GWX, ECO:0007744|PDB:4GWY, ECO:0007744|PDB:4GWZ, ECO:0007744|PDB:4GX3, ECO:0007744|PDB:4GX4, ECO:0007744|PDB:4GX6, ECO:0007744|PDB:4H45, ECO:0007744|PDB:4H46, ECO:0007744|PDB:4KXP, ECO:0007744|PDB:5FBP
source Swiss-Prot : SWS_FT_FI3
53) chain B
residue 244
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:10913263, ECO:0000269|PubMed:12595528, ECO:0000269|PubMed:1312721, ECO:0000269|PubMed:14530289, ECO:0000269|PubMed:15767255, ECO:0000269|PubMed:17933867, ECO:0000269|PubMed:1849642, ECO:0000269|PubMed:2157849, ECO:0000269|PubMed:2164670, ECO:0007744|PDB:1CNQ, ECO:0007744|PDB:1EYI, ECO:0007744|PDB:1EYJ, ECO:0007744|PDB:1EYK, ECO:0007744|PDB:1FBP, ECO:0007744|PDB:1FJ6, ECO:0007744|PDB:1FJ9, ECO:0007744|PDB:1FSA, ECO:0007744|PDB:1KZ8, ECO:0007744|PDB:1LEV, ECO:0007744|PDB:1NUW, ECO:0007744|PDB:1NUX, ECO:0007744|PDB:1NUY, ECO:0007744|PDB:1NUZ, ECO:0007744|PDB:1NV0, ECO:0007744|PDB:1NV1, ECO:0007744|PDB:1NV2, ECO:0007744|PDB:1NV3, ECO:0007744|PDB:1NV4, ECO:0007744|PDB:1NV5, ECO:0007744|PDB:1NV6, ECO:0007744|PDB:1NV7, ECO:0007744|PDB:1Q9D, ECO:0007744|PDB:1RDY, ECO:0007744|PDB:1RDZ, ECO:0007744|PDB:1YXI, ECO:0007744|PDB:1YYZ, ECO:0007744|PDB:1YZ0, ECO:0007744|PDB:2F3B, ECO:0007744|PDB:2F3D, ECO:0007744|PDB:4GBV, ECO:0007744|PDB:4GBW, ECO:0007744|PDB:4GWS, ECO:0007744|PDB:4GWW, ECO:0007744|PDB:4GWX, ECO:0007744|PDB:4GWY, ECO:0007744|PDB:4GWZ, ECO:0007744|PDB:4GX3, ECO:0007744|PDB:4GX4, ECO:0007744|PDB:4GX6, ECO:0007744|PDB:4H45, ECO:0007744|PDB:4H46, ECO:0007744|PDB:4KXP, ECO:0007744|PDB:5FBP
source Swiss-Prot : SWS_FT_FI4
54) chain B
residue 265
type BINDING
sequence P
description BINDING => ECO:0000269|PubMed:10913263, ECO:0000269|PubMed:12595528, ECO:0000269|PubMed:1312721, ECO:0000269|PubMed:14530289, ECO:0000269|PubMed:15767255, ECO:0000269|PubMed:17933867, ECO:0000269|PubMed:1849642, ECO:0000269|PubMed:2157849, ECO:0000269|PubMed:2164670, ECO:0007744|PDB:1CNQ, ECO:0007744|PDB:1EYI, ECO:0007744|PDB:1EYJ, ECO:0007744|PDB:1EYK, ECO:0007744|PDB:1FJ6, ECO:0007744|PDB:1FJ9, ECO:0007744|PDB:1FPB, ECO:0007744|PDB:1FRP, ECO:0007744|PDB:1FSA, ECO:0007744|PDB:1KZ8, ECO:0007744|PDB:1LEV, ECO:0007744|PDB:1NUW, ECO:0007744|PDB:1NUX, ECO:0007744|PDB:1NUY, ECO:0007744|PDB:1NUZ, ECO:0007744|PDB:1NV0, ECO:0007744|PDB:1NV1, ECO:0007744|PDB:1NV2, ECO:0007744|PDB:1NV3, ECO:0007744|PDB:1NV4, ECO:0007744|PDB:1NV5, ECO:0007744|PDB:1NV6, ECO:0007744|PDB:1NV7, ECO:0007744|PDB:1Q9D, ECO:0007744|PDB:1RDY, ECO:0007744|PDB:1RDZ, ECO:0007744|PDB:1YXI, ECO:0007744|PDB:1YYZ, ECO:0007744|PDB:1YZ0, ECO:0007744|PDB:2F3B, ECO:0007744|PDB:2F3D, ECO:0007744|PDB:2QVU, ECO:0007744|PDB:2QVV, ECO:0007744|PDB:4GBV, ECO:0007744|PDB:4GBW, ECO:0007744|PDB:4GWS, ECO:0007744|PDB:4GWU, ECO:0007744|PDB:4GWW, ECO:0007744|PDB:4GWX, ECO:0007744|PDB:4GWY, ECO:0007744|PDB:4GWZ, ECO:0007744|PDB:4GX3, ECO:0007744|PDB:4GX4, ECO:0007744|PDB:4GX6, ECO:0007744|PDB:4H45, ECO:0007744|PDB:4H46, ECO:0007744|PDB:4KXP, ECO:0007744|PDB:5FBP
source Swiss-Prot : SWS_FT_FI5
55) chain B
residue 275
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:10913263, ECO:0000269|PubMed:12595528, ECO:0000269|PubMed:1312721, ECO:0000269|PubMed:14530289, ECO:0000269|PubMed:15767255, ECO:0000269|PubMed:17933867, ECO:0000269|PubMed:1849642, ECO:0000269|PubMed:2157849, ECO:0000269|PubMed:2164670, ECO:0007744|PDB:1CNQ, ECO:0007744|PDB:1EYI, ECO:0007744|PDB:1EYJ, ECO:0007744|PDB:1EYK, ECO:0007744|PDB:1FBP, ECO:0007744|PDB:1FJ6, ECO:0007744|PDB:1FJ9, ECO:0007744|PDB:1FSA, ECO:0007744|PDB:1KZ8, ECO:0007744|PDB:1LEV, ECO:0007744|PDB:1NUW, ECO:0007744|PDB:1NUX, ECO:0007744|PDB:1NUY, ECO:0007744|PDB:1NUZ, ECO:0007744|PDB:1NV0, ECO:0007744|PDB:1NV1, ECO:0007744|PDB:1NV2, ECO:0007744|PDB:1NV3, ECO:0007744|PDB:1NV4, ECO:0007744|PDB:1NV5, ECO:0007744|PDB:1NV7, ECO:0007744|PDB:1Q9D, ECO:0007744|PDB:1RDY, ECO:0007744|PDB:1RDZ, ECO:0007744|PDB:1YXI, ECO:0007744|PDB:1YYZ, ECO:0007744|PDB:1YZ0, ECO:0007744|PDB:2F3B, ECO:0007744|PDB:2F3D, ECO:0007744|PDB:4GBW, ECO:0007744|PDB:4GWS, ECO:0007744|PDB:4GWW, ECO:0007744|PDB:4GWX, ECO:0007744|PDB:4GWZ, ECO:0007744|PDB:4GX3, ECO:0007744|PDB:4GX4, ECO:0007744|PDB:4GX6, ECO:0007744|PDB:4H45, ECO:0007744|PDB:4H46, ECO:0007744|PDB:4KXP, ECO:0007744|PDB:5FBP
source Swiss-Prot : SWS_FT_FI6
56) chain B
residue 151
type MOD_RES
sequence D
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI8
57) chain B
residue 208
type MOD_RES
sequence I
description Phosphoserine; by PKA => ECO:0000269|PubMed:6296821
source Swiss-Prot : SWS_FT_FI9

Display surface

Download
Links