Target Binding Site Detail

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Target General Information
Ligand General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T63068 Target Info
Target Name Serum albumin (ALB)
Synonyms Serum albumin
Target Type Successful Target
Gene Name ALB
UniProt ID
ALBU_HUMAN
Ligand General Information  Top
Ligand Name Levothyroxine Ligand Info
Canonical SMILES C1=C(C=C(C(=C1I)OC2=CC(=C(C(=C2)I)O)I)I)CC(C(=O)O)N
InChI 1S/C15H11I4NO4/c16-8-4-7(5-9(17)13(8)21)24-14-10(18)1-6(2-11(14)19)3-12(20)15(22)23/h1-2,4-5,12,21H,3,20H2,(H,22,23)/t12-/m0/s1
InChIKey XUIIKFGFIJCVMT-LBPRGKRZSA-N
PubChem Compound ID 5819
Drug Binding Sites of Target  Top
PDB ID: 1HK4      HUMAN SERUM ALBUMIN COMPLEXED WITH THYROXINE (3,3',5,5'-TETRAIODO-L-THYRONINE) and myristic acid (tetradecanoic acid)
Method X-ray diffraction Resolution 2.40 Å Mutation No [1]
PDB Sequence
HKSEVAHRFK
12
DLGEENFKAL
22
VLIAFAQYLQ
32
QCPFEDHVKL
42
VNEVTEFAKT
52

CVADESAENC
62
DKSLHTLFGD
72
KLCTVATLRE
82
TYGEMADCCA
92
KQEPERNECF
102

LQHKDDNPNL
112
PRLVRPEVDV
122
MCTAFHDNEE
132
TFLKKYLYEI
142
ARRHPYFYAP
152

ELLFFAKRYK
162
AAFTECCQAA
172
DKAACLLPKL
182
DELRDEGKAS
192
SAKQRLKCAS
202

LQKFGERAFK
212
AWAVARLSQR
222
FPKAEFAEVS
232
KLVTDLTKVH
242
TECCHGDLLE
252

CADDRADLAK
262
YICENQDSIS
272
SKLKECCEKP
282
LLEKSHCIAE
292
VENDEMPADL
302

PSLAADFVES
312
KDVCKNYAEA
322
KDVFLGMFLY
332
EYARRHPDYS
342
VVLLLRLAKT
352

YETTLEKCCA
362
AADPHECYAK
372
VFDEFKPLVE
382
EPQNLIKQNC
392
ELFEQLGEYK
402

FQNALLVRYT
412
KKVPQVSTPT
422
LVEVSRNLGK
432
VGSKCCKHPE
442
AKRMPCAEDY
452

LSVVLNQLCV
462
LHEKTPVSDR
472
VTKCCTESLV
482
NRRPCFSALE
492
VDETYVPKEF
502

NAETFTFHAD
512
ICTLSEKERQ
522
IKKQTALVEL
532
VKHKPKATKE
542
QLKAVMDDFA
552

AFVEKCCKAD
562
DKETCFAEEG
572
KKLVAASQAA
582
LG
Residue
Distance (Å)
GLU184
4.640
ASP187
3.579
GLU188
3.738
LYS190
3.264
ALA191
3.451
LYS195
3.387
GLU425
3.700
ASN429
2.886
Residue
Distance (Å)
LYS432
3.230
VAL433
4.084
LYS436
3.235
ASP451
3.667
TYR452
3.246
VAL455
3.619
VAL456
4.370
PDB ID: 1HK1      HUMAN SERUM ALBUMIN COMPLEXED WITH THYROXINE (3,3',5,5'-TETRAIODO-L-THYRONINE)
Method X-ray diffraction Resolution 2.65 Å Mutation No [1]
PDB Sequence
SEVAHRFKDL
14
GEENFKALVL
24
IAFAQYLQQC
34
PFEDHVKLVN
44
EVTEFAKTCV
54

ADESAENCDK
64
SLHTLFGDKL
74
CTDCCAKQEP
96
ERNECFLQHK
106
DDNPNLPRLV
116

RPEVDVMCTA
126
FHDNEETFLK
136
KYLYEIARRH
146
PYFYAPELLF
156
FAKRYKAAFT
166

ECCQAADKAA
176
CLLPKLDELR
186
DEGKASSAKQ
196
RLKCASLQKF
206
GERAFKAWAV
216

ARLSQRFPKA
226
EFAEVSKLVT
236
DLTKVHTECC
246
HGDLLECADD
256
RADLAKYICE
266

NQDSISSKLK
276
ECCEKPLLEK
286
SHCIAEVEND
296
EMPADLPSLA
306
ADFVESKDVC
316

KNYAEAKDVF
326
LGMFLYEYAR
336
RHPDYSVVLL
346
LRLAKTYETT
356
LEKCCAAADP
366

HECYAKVFDE
376
FKPLVEEPQN
386
LIKQNCELFE
396
QLGEYKFQNA
406
LLVRYTKKVP
416

QVSTPTLVEV
426
SRNLGKVGSK
436
CCKHPEAKRM
446
PCAEDYLSVV
456
LNQLCVLHEK
466

TPVSDRVTKC
476
CTESLVNRRP
486
CFSALEVDET
496
YVPKEFNAET
506
FTFHADICTL
516

SEKERQIKKQ
526
TALVELVKHK
536
PKATKEQLKA
546
VMDDFAAFVE
556
KCCKADDKET
566

CFA
Residue
Distance (Å)
TYR150
3.161
LYS195
3.668
GLN196
4.745
LYS199
2.771
PHE211
4.385
TRP214
3.569
ALA215
4.398
ARG218
3.018
LEU219
3.515
ARG222
2.894
PHE223
4.734
LEU238
3.196
HIS242
3.829
ARG257
2.649
LEU260
4.114
SER287
4.453
ILE290
3.242
ALA291
3.724
GLU292
4.725
VAL293
4.322
LEU387
3.388
GLN390
3.607
ASN391
3.220
LEU394
3.842
PHE403
4.778
ALA406
3.516
LEU407
3.322
ARG410
3.415
TYR411
2.862
Residue
Distance (Å)
LYS414
3.695
LEU430
4.947
LEU453
3.855
PHE488
4.917
SER489
2.694
PHE502
3.805
GLU505
4.163
THR506
3.034
PHE507
3.302
THR508
2.725
PHE509
4.421
HIS510
3.746
ILE513
3.463
LEU516
4.695
ARG521
4.840
LYS524
3.467
LYS525
3.680
THR527
4.259
ALA528
2.736
LEU529
4.858
GLU531
3.679
LEU532
3.116
HIS535
4.056
VAL547
3.416
MET548
3.620
PHE551
3.378
ALA552
3.983
VAL555
3.899
PHE568
3.687
PDB ID: 1HK5      HUMAN SERUM ALBUMIN MUTANT R218H COMPLEXED WITH THYROXINE (3,3',5,5'-TETRAIODO-L-THYRONINE) and myristic acid (tetradecanoic acid)
Method X-ray diffraction Resolution 2.70 Å Mutation Yes [1]
PDB Sequence
HKSEVAHRFK
12
DLGEENFKAL
22
VLIAFAQYLQ
32
QCPFEDHVKL
42
VNEVTEFAKT
52

CVADESAENC
62
DKSLHTLFGD
72
KLCTVATLRE
82
TYGEMADCCA
92
KQEPERNECF
102

LQHKDDNPNL
112
PRLVRPEVDV
122
MCTAFHDNEE
132
TFLKKYLYEI
142
ARRHPYFYAP
152

ELLFFAKRYK
162
AAFTECCQAA
172
DKAACLLPKL
182
DELRDEGKAS
192
SAKQRLKCAS
202

LQKFGERAFK
212
AWAVAHLSQR
222
FPKAEFAEVS
232
KLVTDLTKVH
242
TECCHGDLLE
252

CADDRADLAK
262
YICENQDSIS
272
SKLKECCEKP
282
LLEKSHCIAE
292
VENDEMPADL
302

PSLAADFVES
312
KDVCKNYAEA
322
KDVFLGMFLY
332
EYARRHPDYS
342
VVLLLRLAKT
352

YETTLEKCCA
362
AADPHECYAK
372
VFDEFKPLVE
382
EPQNLIKQNC
392
ELFEQLGEYK
402

FQNALLVRYT
412
KKVPQVSTPT
422
LVEVSRNLGK
432
VGSKCCKHPE
442
AKRMPCAEDY
452

LSVVLNQLCV
462
LHEKTPVSDR
472
VTKCCTESLV
482
NRRPCFSALE
492
VDETYVPKEF
502

NAETFTFHAD
512
ICTLSEKERQ
522
IKKQTALVEL
532
VKHKPKATKE
542
QLKAVMDDFA
552

AFVEKCCKAD
562
DKETCFAEEG
572
KKLVAASQAA
582
LG
Residue
Distance (Å)
GLU184
4.797
ASP187
3.820
GLU188
3.757
LYS190
3.782
ALA191
3.489
LYS195
3.497
GLU425
3.897
ARG428
4.664
ASN429
2.993
Residue
Distance (Å)
LYS432
3.154
VAL433
3.931
LYS436
4.006
ASP451
3.624
TYR452
3.525
VAL455
3.530
VAL456
4.437
GLN459
4.990
PDB ID: 1HK2      HUMAN SERUM ALBUMIN MUTANT R218H COMPLEXED WITH THYROXINE (3,3',5,5'-TETRAIODO-L-THYRONINE)
Method X-ray diffraction Resolution 2.80 Å Mutation Yes [1]
PDB Sequence
SEVAHRFKDL
14
GEENFKALVL
24
IAFAQYLQQC
34
PFEDHVKLVN
44
EVTEFAKTCV
54

ADESAENCDK
64
SLHTLFGDKL
74
CTDCCAKQEP
96
ERNECFLQHK
106
DDNPNLPRLV
116

RPEVDVMCTA
126
FHDNEETFLK
136
KYLYEIARRH
146
PYFYAPELLF
156
FAKRYKAAFT
166

ECCQAADKAA
176
CLLPKLDELR
186
DEGKASSAKQ
196
RLKCASLQKF
206
GERAFKAWAV
216

AHLSQRFPKA
226
EFAEVSKLVT
236
DLTKVHTECC
246
HGDLLECADD
256
RADLAKYICE
266

NQDSISSKLK
276
ECCEKPLLEK
286
SHCIAEVEND
296
EMPADLPSLA
306
ADFVESKDVC
316

KNYAEAKDVF
326
LGMFLYEYAR
336
RHPDYSVVLL
346
LRLAKTYETT
356
LEKCCAAADP
366

HECYAKVFDE
376
FKPLVEEPQN
386
LIKQNCELFE
396
QLGEYKFQNA
406
LLVRYTKKVP
416

QVSTPTLVEV
426
SRNLGKVGSK
436
CCKHPEAKRM
446
PCAEDYLSVV
456
LNQLCVLHEK
466

TPVSDRVTKC
476
CTESLVNRRP
486
CFSALEVDET
496
YVPKEFNAET
506
FTFHADICTL
516

SEKERQIKKQ
526
TALVELVKHK
536
PKATKEQLKA
546
VMDDFAAFVE
556
KCCKADDKET
566

CFAEEGKKLV
576
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .T44 or .T442 or .T443 or :3T44;style chemicals stick;color identity;select .A:150 or .A:195 or .A:196 or .A:199 or .A:211 or .A:214 or .A:215 or .A:218 or .A:219 or .A:222 or .A:223 or .A:238 or .A:242 or .A:257 or .A:260 or .A:264 or .A:287 or .A:290 or .A:291 or .A:293 or .A:387 or .A:390 or .A:391 or .A:394 or .A:403 or .A:406 or .A:407 or .A:410 or .A:411 or .A:414 or .A:430 or .A:453 or .A:485 or .A:488 or .A:489 or .A:502 or .A:505 or .A:506 or .A:507 or .A:508 or .A:509 or .A:510 or .A:513 or .A:516 or .A:521 or .A:524 or .A:525 or .A:527 or .A:528 or .A:529 or .A:531 or .A:532 or .A:535 or .A:547 or .A:548 or .A:551 or .A:552 or .A:554 or .A:555 or .A:568 or .A:575 or .A:576; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
TYR150
3.020
LYS195
4.423
GLN196
4.629
LYS199
2.650
PHE211
4.272
TRP214
4.022
ALA215
4.193
HIS218
3.213
LEU219
3.777
ARG222
3.338
PHE223
4.989
LEU238
3.438
HIS242
3.947
ARG257
2.695
LEU260
4.396
ILE264
4.938
SER287
4.551
ILE290
3.294
ALA291
3.735
VAL293
4.295
LEU387
3.335
GLN390
3.404
ASN391
3.068
LEU394
3.420
PHE403
4.626
ALA406
3.720
LEU407
3.322
ARG410
4.038
TYR411
2.564
LYS414
3.431
LEU430
4.899
Residue
Distance (Å)
LEU453
3.946
ARG485
4.737
PHE488
4.946
SER489
2.747
PHE502
3.727
GLU505
4.320
THR506
3.377
PHE507
3.203
THR508
2.844
PHE509
4.403
HIS510
4.033
ILE513
3.385
LEU516
4.277
ARG521
4.722
LYS524
3.215
LYS525
3.884
THR527
4.225
ALA528
2.647
LEU529
4.746
GLU531
3.514
LEU532
3.132
HIS535
4.019
VAL547
3.331
MET548
3.617
PHE551
3.440
ALA552
4.015
PHE554
4.807
VAL555
4.064
PHE568
3.921
LEU575
4.097
VAL576
3.281
PDB ID: 1HK3      Human serum albumin mutant r218p complexed with thyroxine (3,3',5,5'-tetraiodo-l-thyronine)
Method X-ray diffraction Resolution 2.80 Å Mutation Yes [1]
PDB Sequence
SEVAHRFKDL
14
GEENFKALVL
24
IAFAQYLQQC
34
PFEDHVKLVN
44
EVTEFAKTCV
54

ADESAENCDK
64
SLHTLFGDKL
74
CTDCCAKQEP
96
ERNECFLQHK
106
DDNPNLPRLV
116

RPEVDVMCTA
126
FHDNEETFLK
136
KYLYEIARRH
146
PYFYAPELLF
156
FAKRYKAAFT
166

ECCQAADKAA
176
CLLPKLDELR
186
DEGKASSAKQ
196
RLKCASLQKF
206
GERAFKAWAV
216

APLSQRFPKA
226
EFAEVSKLVT
236
DLTKVHTECC
246
HGDLLECADD
256
RADLAKYICE
266

NQDSISSKLK
276
ECCEKPLLEK
286
SHCIAEVEND
296
EMPADLPSLA
306
ADFVESKDVC
316

KNYAEAKDVF
326
LGMFLYEYAR
336
RHPDYSVVLL
346
LRLAKTYETT
356
LEKCCAAADP
366

HECYAKVFDE
376
FKPLVEEPQN
386
LIKQNCELFE
396
QLGEYKFQNA
406
LLVRYTKKVP
416

QVSTPTLVEV
426
SRNLGKVGSK
436
CCKHPEAKRM
446
PCAEDYLSVV
456
LNQLCVLHEK
466

TPVSDRVTKC
476
CTESLVNRRP
486
CFSALEVDET
496
YVPKEFNAET
506
FTFHADICTL
516

SEKERQIKKQ
526
TALVELVKHK
536
PKATKEQLKA
546
VMDDFAAFVE
556
KCCKADDKET
566

CFAEEGKKL
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .T44 or .T442 or .T443 or :3T44;style chemicals stick;color identity;select .A:150 or .A:195 or .A:196 or .A:199 or .A:211 or .A:214 or .A:215 or .A:218 or .A:219 or .A:222 or .A:223 or .A:238 or .A:242 or .A:257 or .A:260 or .A:287 or .A:290 or .A:291 or .A:293 or .A:387 or .A:390 or .A:391 or .A:394 or .A:403 or .A:406 or .A:407 or .A:410 or .A:411 or .A:414 or .A:430 or .A:453 or .A:489 or .A:502 or .A:505 or .A:506 or .A:507 or .A:508 or .A:509 or .A:510 or .A:513 or .A:516 or .A:521 or .A:524 or .A:525 or .A:527 or .A:528 or .A:531 or .A:532 or .A:535 or .A:547 or .A:548 or .A:551 or .A:552 or .A:555 or .A:568 or .A:575; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
TYR150
3.005
LYS195
3.421
GLN196
4.691
LYS199
2.969
PHE211
4.697
TRP214
3.455
ALA215
4.406
PRO218
3.224
LEU219
3.540
ARG222
3.332
PHE223
4.894
LEU238
3.346
HIS242
3.818
ARG257
3.049
LEU260
4.609
SER287
4.596
ILE290
3.409
ALA291
3.863
VAL293
4.268
LEU387
3.478
GLN390
3.220
ASN391
3.293
LEU394
4.093
PHE403
4.674
ALA406
3.532
LEU407
3.394
ARG410
3.175
TYR411
2.763
Residue
Distance (Å)
LYS414
3.811
LEU430
4.704
LEU453
3.985
SER489
2.681
PHE502
3.790
GLU505
4.294
THR506
3.407
PHE507
3.273
THR508
2.686
PHE509
4.367
HIS510
4.002
ILE513
3.936
LEU516
4.706
ARG521
4.889
LYS524
3.143
LYS525
3.796
THR527
4.112
ALA528
3.141
GLU531
3.725
LEU532
3.340
HIS535
4.155
VAL547
3.317
MET548
3.805
PHE551
3.556
ALA552
4.231
VAL555
4.058
PHE568
4.044
LEU575
3.354
References  Top
REF 1 Structural basis of albumin-thyroxine interactions and familial dysalbuminemic hyperthyroxinemia. Proc Natl Acad Sci U S A. 2003 May 27;100(11):6440-5.

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