|
|
eF-site ID
|
5q0c-D |
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PDB Code
|
5q0c |
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Chain
|
D |
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click to enlarge
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Title
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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 |
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Classification
|
HYDROLASE/HYDROLASE INHIBITOR |
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Compound
|
Fructose-1,6-bisphosphatase isozyme 2 |
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Source
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(F16P2_HUMAN) |
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Sequence
|
D: |
TDMLTLTRYVMEKGRQAKGTGELTQLLNSMLTAIKAISSA
VRKAGLAHLYGIAGSVNVKLDVLSNSLVINMLQSSYSTCV
LVSEENKDAIITAKEKRGKYVVCFDPLDGSSNIDCLASIG
TIFAIYRKTSEDEPSEKDALQCGRNIVAAGYALYGSATLV
ALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIYSLNE
GYAKYFDAATTEYVQKKKFPEDGSAPYGARYVGSMVADVH
RTLVYGGIFLYPANQKSPKGKLRLLYECNPVAYIIEQAGG
LATTGTQPVLDVKPEAIHQRVPLILGSPEDVQEYLTCVQK
NQ
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Description
|
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Functional site
|
|
|
1)
|
chain |
D |
| residue |
98 |
| type |
BINDING |
| sequence |
E
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
2)
|
chain |
D |
| residue |
119 |
| type |
BINDING |
| sequence |
D
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
3)
|
chain |
D |
| residue |
121 |
| type |
BINDING |
| sequence |
L
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
4)
|
chain |
D |
| residue |
122 |
| type |
BINDING |
| sequence |
D
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
5)
|
chain |
D |
| residue |
213 |
| type |
BINDING |
| sequence |
N
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
6)
|
chain |
D |
| residue |
245 |
| type |
BINDING |
| sequence |
Y
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
7)
|
chain |
D |
| residue |
265 |
| type |
BINDING |
| sequence |
Y
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
8)
|
chain |
D |
| residue |
275 |
| type |
BINDING |
| sequence |
K
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
9)
|
chain |
D |
| residue |
281 |
| type |
BINDING |
| sequence |
E
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
10)
|
chain |
D |
| 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
|
|
|
11)
|
chain |
D |
| residue |
216 |
| type |
MOD_RES |
| sequence |
Y
|
| description |
Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1N1
|
| source |
Swiss-Prot : SWS_FT_FI4
|
|
|
12)
|
chain |
D |
| residue |
219 |
| type |
MOD_RES |
| sequence |
Y
|
| description |
Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1N1
|
| source |
Swiss-Prot : SWS_FT_FI4
|
|
|
13)
|
chain |
D |
| residue |
18 |
| type |
BINDING |
| sequence |
V
|
| description |
BINDING => ECO:0000269|PubMed:22120740
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
14)
|
chain |
D |
| residue |
28 |
| type |
BINDING |
| sequence |
T
|
| description |
BINDING => ECO:0000269|PubMed:22120740
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
15)
|
chain |
D |
| residue |
113 |
| type |
BINDING |
| sequence |
K
|
| description |
BINDING => ECO:0000269|PubMed:22120740
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
16)
|
chain |
D |
| residue |
141 |
| type |
BINDING |
| sequence |
R
|
| description |
BINDING => ECO:0000269|PubMed:22120740
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
|