Binding Site Information of Target

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Target General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T56545 Target Info
Target Name Apolipoprotein A-I (APOA1)
Synonyms Truncated apolipoprotein AI; Apolipoprotein A1; ApoAI; ApoA-I; Apo-AI
Target Type Clinical trial Target
Gene Name APOA1
Biochemical Class Apolipoprotein
UniProt ID
APOA1_HUMAN
Drug Binding Sites of Target  Top
Ligand Name: Cholesterol Ligand Info
Structure Description Solution structure of double super helix model PDB:3K2S
Method Solution scattering Resolution N.A. Mutation No [1]
PDB Sequence
DEPPQSPWDR
10
VKDLATVYVD
20
VLKDSGRDYV
30
SQFEGSALGK
40
QLNLKLLDNW
50

DSVTSTFSKL
60
REQLGPVTQE
70
FWDNLEKETE
80
GLRQEMSKDL
90
EEVKAKVQPY
100

LDDFQKKWQE
110
EMELYRQKVE
120
PLRAELQEGA
130
RQKLHELQEK
140
LSPLGEEMRD
150

RARAHVDALR
160
THLAPYSDEL
170
RQRLAARLEA
180
LKENGGARLA
190
EYHAKATEHL
200

STLSEKAKPA
210
LEDLRQGLLP
220
VLESFKVSFL
230
SALEEYTKKL
240
NTQ
Residue
Distance (Å)
THR202
4.101
LEU203
3.305
LYS206
3.488
ALA207
4.588
Residue
Distance (Å)
ALA210
3.519
ASP213
3.414
LEU214
3.576
Ligand Name: 1,2-Dimyristoyl-sn-glycero-3-phosphocholine Ligand Info
Structure Description MT1-MMP HPX Domain with Blade 2 Loop Bound to Nanodiscs PDB:6CM1
Method Solution NMR Resolution N.A. Mutation No [2]
PDB Sequence
STFSKLREQL
64
GPVTQEFWDN
74
LEKETEGLRQ
84
EMSKDLEEVK
94
AKVQPYLDDF
104

QKKWQEEMEL
114
YRQKVEPYLD
124
DFQKKWQEEM
134
ELYRQKVEPL
144
RAELQEGARQ
154

KLHELQEKLS
164
PLGEEMRDRA
174
RAHVDALRTH
184
LAPYSDELRQ
194
RLAARLEALK
204

ENGGARLAEY
214
HAKATEHLST
224
LSEKAKPALE
234
DLRQGLLPVL
244
ESFKVSFLSA
254

LEEYTKKLNT
264
Q
Residue
Distance (Å)
SER55
1.666
PHE57
2.257
SER58
2.230
ARG61
1.642
THR68
3.307
GLN69
4.754
TRP72
2.084
ASP73
4.931
LEU75
2.169
GLU76
2.068
LYS77
3.913
THR79
2.406
GLU80
2.069
ARG83
1.616
GLN84
4.543
MET86
2.259
LEU90
2.296
LYS94
1.716
GLN98
4.130
LEU101
4.290
ASP102
2.871
GLN105
2.554
TRP108
2.091
GLN109
2.101
MET112
2.179
GLU113
2.624
TYR115
2.419
ARG116
2.103
VAL119
3.261
GLU120
2.604
LEU123
2.497
ASP124
3.562
PHE126
2.717
GLN127
2.622
TRP130
2.228
GLN131
4.036
MET134
2.313
TYR137
2.004
ARG138
2.220
GLN139
4.700
VAL141
2.517
GLU142
3.682
ARG145
1.783
ALA146
4.388
LEU148
2.346
GLN149
2.869
ALA152
2.282
ARG153
2.414
LYS155
2.594
LEU156
2.157
HIS157
4.932
LEU159
2.221
GLN160
2.325
GLU161
4.457
LEU163
2.489
SER164
2.360
LEU166
2.255
GLY167
2.197
GLU168
4.083
MET170
2.118
ARG171
2.704
ASP172
4.327
ARG173
3.628
Residue
Distance (Å)
ALA174
2.453
ARG175
2.252
HIS177
2.499
VAL178
2.278
ASP179
4.840
LEU181
2.418
ARG182
2.175
THR183
4.979
LEU185
2.149
ALA186
2.284
TYR188
2.892
SER189
2.385
ASP190
4.712
LEU192
2.723
ARG193
1.874
GLN194
2.246
LEU196
2.484
ALA197
2.726
ARG199
4.912
LEU200
2.081
GLU201
4.790
LEU203
2.288
LYS204
2.044
GLU205
4.396
ASN206
4.730
GLY207
2.420
GLY208
2.193
ALA209
4.795
ARG210
2.219
LEU211
2.289
TYR214
2.480
HIS215
2.259
ALA218
2.678
THR219
3.890
LEU222
2.203
SER223
2.020
THR224
4.299
LEU225
2.226
SER226
2.061
GLU227
2.415
LYS228
2.626
ALA229
2.344
LYS230
3.473
ALA232
2.561
LEU233
2.154
LEU236
2.238
ARG237
2.353
LEU240
2.024
LEU241
3.085
VAL243
2.494
LEU244
2.094
PHE247
2.279
LYS248
1.920
SER250
2.153
PHE251
2.269
LEU252
2.919
ALA254
2.475
LEU255
2.212
TYR258
1.703
LYS261
3.864
LEU262
2.575
GLN265
2.521
Ligand Name: 1,2-Dioleoyl-sn-glycero-3-phosphoethanolamine Ligand Info
Structure Description Cryo-EM structure of SARS-CoV-2 ORF3a PDB:7KJR
Method Electron microscopy Resolution 2.08 Å Mutation No [3]
PDB Sequence
FSKLREQLGP
34
VTQEFWDNLE
44
KETEGLRQEM
54
S
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set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .PEE or .PEE2 or .PEE3 or :3PEE;style chemicals stick;color identity;select .C:32 or .C:36 or .C:39 or .C:40; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU32
3.751
THR36
3.359
Residue
Distance (Å)
PHE39
4.114
TRP40
2.932
Ligand Name: 2-[hydroxy-[(2R)-3-[(Z)-octadec-9-enoyl]oxy-2-propanoyloxypropoxy]phosphoryl]oxyethyl-trimethylazanium Ligand Info
Structure Description NMR-driven structure of the KRAS4B-G12D "alpha-beta" dimer on a lipid bilayer nanodisc PDB:7RSE
Method Solution NMR Resolution N.A. Mutation Yes [4]
PDB Sequence
STFSKLREQL
264
GPVTQEFWDN
274
LEKETEGLRQ
284
EMSKDLEEVK
294
AKVQPYLDDF
304

QKKWQEEMEL
314
YRQKVEPLRA
324
ELQEGARQKL
334
HELQEKLSPL
344
GEEMRDRARA
354

HVDALRTHLA
364
PYSDELRQRL
374
AARLEALKEN
384
GGARLAEYHA
394
KATEHLSTLS
404

EKAKPALEDL
414
RQGLLPVLES
424
FKVSFLSALE
434
EYTKKLN
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set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .7Q9 or .7Q92 or .7Q93 or :37Q9;style chemicals stick;color identity;select .D:257 or .D:258 or .D:259 or .D:261 or .D:262 or .D:265 or .D:269 or .D:272 or .D:276 or .D:280 or .D:283 or .D:284 or .D:287 or .D:290 or .D:291 or .D:294 or .D:298 or .D:301 or .D:302 or .D:305 or .D:315 or .D:319 or .D:323 or .D:330 or .D:331 or .D:332 or .D:333 or .D:334 or .D:335 or .D:338 or .D:342 or .D:346 or .D:349 or .D:352 or .D:353 or .D:360 or .D:367 or .D:370 or .D:371 or .D:374 or .D:375 or .D:378 or .D:382 or .D:389 or .D:392 or .D:393 or .D:396 or .D:397 or .D:399 or .D:400 or .D:401 or .D:403 or .D:404 or .D:433 or .D:436 or .D:437 or .D:440; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE257
3.310
SER258
3.390
LYS259
3.971
ARG261
2.918
GLU262
4.699
GLY265
4.212
GLN269
4.512
TRP272
3.870
GLU276
4.916
GLU280
3.113
ARG283
3.263
GLN284
4.831
SER287
4.241
LEU290
3.261
GLU291
3.588
LYS294
2.058
GLN298
2.701
LEU301
3.321
ASP302
3.824
GLN305
3.283
TYR315
3.884
VAL319
3.484
ARG323
3.471
ALA330
2.975
ARG331
3.229
GLN332
4.964
LYS333
4.158
LEU334
3.080
HIS335
1.857
Residue
Distance (Å)
GLN338
3.629
SER342
4.444
GLU346
3.339
ARG349
2.925
ALA352
4.139
ARG353
3.497
ARG360
4.170
SER367
3.608
LEU370
4.965
ARG371
3.337
LEU374
3.316
ALA375
3.155
LEU378
4.364
LYS382
1.717
LEU389
3.138
TYR392
3.309
HIS393
2.945
ALA396
3.309
THR397
4.499
HIS399
4.732
LEU400
3.156
SER401
3.232
LEU403
3.700
SER404
2.380
LEU433
3.603
TYR436
3.396
THR437
3.585
LEU440
3.292
Ligand Name: [(2S)-2-azaniumyl-2-carboxyethyl] [(2R)-2,3-bis[[(Z)-octadec-9-enoyl]oxy]propyl] phosphate Ligand Info
Structure Description NMR data-driven model of GTPase KRas-GDP tethered to a lipid-bilayer nanodisc PDB:2MSC
Method Solution NMR Resolution N.A. Mutation No [5]
PDB Sequence
LKLLDNWDSV
210
TSTFSKLREQ
220
LGPVTQEFWD
230
NLEKETEGLR
240
QEMSKDLEEV
250

KAKVQPYLDD
260
FQKKWQEEME
270
LYRQKVEPLR
280
AELQEGARQK
290
LHELQEKLSP
300

LGEEMRDRAR
310
AHVDALRTHL
320
APYSDELRQR
330
LAARLEALKE
340
NGGARLAEYH
350

AKATEHLSTL
360
SEKAKPALED
370
LRQGLLPVLE
380
SFKVSFLSAL
390
EEYTKKLN
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set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .17F or .17F2 or .17F3 or :317F;style chemicals stick;color identity;select .A:371 or .A:382; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU371
3.996
Residue
Distance (Å)
PHE382
4.637
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References  Top
REF 1 Double superhelix model of high density lipoprotein. J Biol Chem. 2009 Dec 25;284(52):36605-36619.
REF 2 MT1-MMP Binds Membranes by Opposite Tips of Its beta Propeller to Position It for Pericellular Proteolysis. Structure. 2019 Feb 5;27(2):281-292.e6.
REF 3 Cryo-EM structure of SARS-CoV-2 ORF3a in lipid nanodiscs. Nat Struct Mol Biol. 2021 Jul;28(7):573-582.
REF 4 Oncogenic KRAS G12D mutation promotes dimerization through a second, phosphatidylserine-dependent interface: a model for KRAS oligomerization. Chem Sci. 2021 Sep 7;12(38):12827-12837.
REF 5 Oncogenic and RASopathy-associated K-RAS mutations relieve membrane-dependent occlusion of the effector-binding site. Proc Natl Acad Sci U S A. 2015 May 26;112(21):6625-30.

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