|
eF-site ID
|
5q0c-B |
PDB Code
|
5q0c |
Chain
|
B |
|
click to enlarge
|
|
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-[5-(4-methoxyphenyl)thiophen-2-yl]sulfonylurea and with fructose-2,6-diphosphate |
Classification
|
HYDROLASE/HYDROLASE INHIBITOR |
Compound
|
Fructose-1,6-bisphosphatase isozyme 2 |
Source
|
(F16P2_HUMAN) |
|
Sequence
|
B: |
TDMLTLTRYVMEKGRQAKGTGELTQLLNSMLTAIKAISSA
VRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQS
SYSTCVLVSEENKDAIITAKEKRGKYVVCFDPLDGSSNID
CLASIGTIFAIYRKTSEDEPSEKDALQCGRNIVAAGYALY
GSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGK
IYSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYGARYVGS
MVADVHRTLVYGGIFLYPANQKSPKGKLRLLYECNPVAYI
IEQAGGLATTGTQPVLDVKPEAIHQRVPLILGSPEDVQEY
LTCVQKNQ
|
|
Description
|
|
Functional site
|
|
1)
|
chain |
B |
residue |
18 |
type |
BINDING |
sequence |
V
|
description |
BINDING => ECO:0000269|PubMed:22120740
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
2)
|
chain |
B |
residue |
28 |
type |
BINDING |
sequence |
T
|
description |
BINDING => ECO:0000269|PubMed:22120740
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
3)
|
chain |
B |
residue |
113 |
type |
BINDING |
sequence |
K
|
description |
BINDING => ECO:0000269|PubMed:22120740
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
4)
|
chain |
B |
residue |
141 |
type |
BINDING |
sequence |
R
|
description |
BINDING => ECO:0000269|PubMed:22120740
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
5)
|
chain |
B |
residue |
69 |
type |
BINDING |
sequence |
D
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
6)
|
chain |
B |
residue |
98 |
type |
BINDING |
sequence |
E
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
7)
|
chain |
B |
residue |
119 |
type |
BINDING |
sequence |
D
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
8)
|
chain |
B |
residue |
121 |
type |
BINDING |
sequence |
L
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
9)
|
chain |
B |
residue |
122 |
type |
BINDING |
sequence |
D
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
10)
|
chain |
B |
residue |
213 |
type |
BINDING |
sequence |
N
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
11)
|
chain |
B |
residue |
245 |
type |
BINDING |
sequence |
Y
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
12)
|
chain |
B |
residue |
265 |
type |
BINDING |
sequence |
Y
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
13)
|
chain |
B |
residue |
275 |
type |
BINDING |
sequence |
K
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
14)
|
chain |
B |
residue |
281 |
type |
BINDING |
sequence |
E
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
15)
|
chain |
B |
residue |
33 |
type |
SITE |
sequence |
Q
|
description |
Important for the conversion from active R-state to inactive T-state in the presence of AMP
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
16)
|
chain |
B |
residue |
216 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1N1
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
17)
|
chain |
B |
residue |
219 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1N1
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
|
|