Binding Site Information of Target
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T79694 | Target Info | |||
| Target Name | Voltage-gated calcium channel alpha Cav3.3 (CACNA1I) | ||||
| Synonyms | Voltage-gated calcium channel subunit alpha Cav3.3; Voltage-dependent T-type calcium channel subunit alpha-1I; KIAA1120; Ca(v)3.3 | ||||
| Target Type | Literature-reported Target | ||||
| Gene Name | CACNA1I | ||||
| Biochemical Class | Voltage-gated ion channel | ||||
| UniProt ID | |||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| Ligand Name: Pimozide | Ligand Info | |||||
| Structure Description | CryoEM structure of human low-voltage activated T-type calcium channel Cav3.3 in complex with pimozide(PMZ) | PDB:7WLL | ||||
| Method | Electron microscopy | Resolution | 3.60 Å | Mutation | No | [1] |
| PDB Sequence |
TSPRNWCIKM
75 VCNPWFECVS85 MLVILLNCVT95 LGMYQPCDDM105 DCLSDRCKIL115 QVFDDFIFIF 125 FAMEMVLKMV135 ALGIFGKKCY145 LGDTWNRLDF155 FIVMAGMVEY165 SLDLQNINLS 175 AIRTVRVLRP185 LKAINRVPSM195 RILVNLLLDT205 LPMLGNVLLL215 CFFVFFIFGI 225 IGVQLWAGLL235 RNRCFLEENF245 TIQGDVALPP255 YYQPEEDDEM265 PFICSLSGDN 275 GIMGCHEIPP285 LKCVNWNRYY323 NVCRTGSANP333 HKGAINFDNI343 GYAWIVIFQV 353 ITLEGWVEIM363 YYVMDAHSFY373 NFIYFILLII383 VGSFFMINLC393 LVVIATQFSE 403 TKQREHRLML413 RETRAKLRGI636 VDSKYFNRGI646 MMAILVNTVS656 MGIEHHEQPE 666 ELTNILEICN676 VVFTSMFALE686 MILKLAAFGL696 FDYLRNPYNI706 FDSIIVIISI 716 WEIVGQADGG726 LSVLRTFRLL736 RVLKLVRFMP746 ALRRQLVVLM756 KTMDNVATFC 766 MLLMLFIFIF776 SILGMHIFGC786 KFSLRTDTGD796 TVPDRKNFDS806 LLWAIVTVFQ 816 ILTQEDWNVV826 LYNGMASTSP836 WASLYFVALM846 TFGNYVLFNL856 LVAILVEGFQ 866 QTIIAHKLFD1173 YVVLAFIFLN1183 CITIALERPQ1193 IEAGSTERIF1203 LTVSNYIFTA 1213 IFVGEMTLKV1223 VSLGLYFGEQ1233 AYLRSSWNVL1243 DGFLVFVSII1253 DIVVSLASAG 1263 GAKILGVLRV1273 LRLLRTLRPL1283 RVISRAPGLK1293 LVVETLISSL1303 KPIGNIVLIC 1313 CAFFIIFGIL1323 GVQLFKGKFY1333 HCLGVDTRNI1343 TNRSDCMAAN1353 YRWVHHKYNF 1363 DNLGQALMSL1373 FVLASKDGWV1383 NIMYNGLDAV1393 AVDQQPVTNH1403 NPWMLLYFIS 1413 FLLIVSFFVL1423 NMFVGVVVEN1433 FHKCRQHQEA1443 EEARRREEKR1453 LRRLEKKRRK 1463 AQRLPYYATY1473 CHTRLLIHSM1483 CTSHYLDIFI1493 TFIICLNVVT1503 MSLEHYNQPT 1513 SLETALKYCN1523 YMFTTVFVLE1533 AVLKLVAFGL1543 RRFFKDRWNQ1553 LDLAIVLLSV 1563 MGITLEEIEI1573 NAALPINPTI1583 IRIMRVLRIA1593 RVLKLLKMAT1603 GMRALLDTVV 1613 QALPQVGNLG1623 LLFMLLFFIY1633 AALGVELFGK1643 LVCNDENPCE1653 GMSRHATFEN 1663 FGMAFLTLFQ1673 VSTGDNWNGI1683 MKDTLRDCTH1693 DERSCLSSLQ1703 FVSPLYFVSF 1713 VLTAQFVLIN1723 VVVAVLMKHL1733 DDSNK
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|
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PHE387
3.961
ASN391
3.320
LEU394
3.724
PHE815
4.315
LEU818
2.962
THR819
3.809
GLN820
3.959
ASN850
2.026
PHE854
3.337
VAL858
3.470
LYS1379
3.588
|
|||||
| Ligand Name: Mibefradil | Ligand Info | |||||
| Structure Description | CryoEM structure of human low-voltage activated T-type calcium channel Cav3.3 in complex with mibefradil (MIB) | PDB:7WLJ | ||||
| Method | Electron microscopy | Resolution | 3.90 Å | Mutation | No | [1] |
| PDB Sequence |
TSPRNWCIKM
75 VCNPWFECVS85 MLVILLNCVT95 LGMYQPCDDM105 DCLSDRCKIL115 QVFDDFIFIF 125 FAMEMVLKMV135 ALGIFGKKCY145 LGDTWNRLDF155 FIVMAGMVEY165 SLDLQNINLS 175 AIRTVRVLRP185 LKAINRVPSM195 RILVNLLLDT205 LPMLGNVLLL215 CFFVFFIFGI 225 IGVQLWAGLL235 RNRCFLEENF245 TIQGDVALPP255 YYQPEEDDEM265 PFICSLSGDN 275 GIMGCHEIPP285 LKCVNWNRYY323 NVCRTGSANP333 HKGAINFDNI343 GYAWIVIFQV 353 ITLEGWVEIM363 YYVMDAHSFY373 NFIYFILLII383 VGSFFMINLC393 LVVIATQFSE 403 TKQREHRLML413 RETRAKLRGI636 VDSKYFNRGI646 MMAILVNTVS656 MGIEHHEQPE 666 ELTNILEICN676 VVFTSMFALE686 MILKLAAFGL696 FDYLRNPYNI706 FDSIIVIISI 716 WEIVGQADGG726 LSVLRTFRLL736 RVLKLVRFMP746 ALRRQLVVLM756 KTMDNVATFC 766 MLLMLFIFIF776 SILGMHIFGC786 KFSLRTDTGD796 TVPDRKNFDS806 LLWAIVTVFQ 816 ILTQEDWNVV826 LYNGMASTSP836 WASLYFVALM846 TFGNYVLFNL856 LVAILVEGFQ 866 QTIIAHKLFD1173 YVVLAFIFLN1183 CITIALERPQ1193 IEAGSTERIF1203 LTVSNYIFTA 1213 IFVGEMTLKV1223 VSLGLYFGEQ1233 AYLRSSWNVL1243 DGFLVFVSII1253 DIVVSLASAG 1263 GAKILGVLRV1273 LRLLRTLRPL1283 RVISRAPGLK1293 LVVETLISSL1303 KPIGNIVLIC 1313 CAFFIIFGIL1323 GVQLFKGKFY1333 HCLGVDTRNI1343 TNRSDCMAAN1353 YRWVHHKYNF 1363 DNLGQALMSL1373 FVLASKDGWV1383 NIMYNGLDAV1393 AVDQQPVTNH1403 NPWMLLYFIS 1413 FLLIVSFFVL1423 NMFVGVVVEN1433 FHKCRQHQEA1443 EEARRREEKR1453 LRRLEKKRRK 1463 AQRLPYYATY1473 CHTRLLIHSM1483 CTSHYLDIFI1493 TFIICLNVVT1503 MSLEHYNQPT 1513 SLETALKYCN1523 YMFTTVFVLE1533 AVLKLVAFGL1543 RRFFKDRWNQ1553 LDLAIVLLSV 1563 MGITLEEIEI1573 NAALPINPTI1583 IRIMRVLRIA1593 RVLKLLKMAT1603 GMRALLDTVV 1613 QALPQVGNLG1623 LLFMLLFFIY1633 AALGVELFGK1643 LVCNDENPCE1653 GMSRHATFEN 1663 FGMAFLTLFQ1673 VSTGDNWNGI1683 MKDTLRDCTH1693 DERSCLSSLQ1703 FVSPLYFVSF 1713 VLTAQFVLIN1723 VVVAVLMKHL1733 DDSNK
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|
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PHE387
3.769
ILE390
4.075
ASN391
3.308
LEU394
3.558
PHE815
3.451
LEU818
3.427
THR819
3.785
GLN820
4.063
ASN850
2.881
PHE854
3.532
ASN855
4.597
|
|||||
| Ligand Name: 1,2-Distearoyl-sn-glycero-3-phosphoethanolamine | Ligand Info | |||||
| Structure Description | CryoEM structure of human low-voltage activated T-type calcium channel CaV3.3 (apo) | PDB:7WLI | ||||
| Method | Electron microscopy | Resolution | 3.30 Å | Mutation | No | [1] |
| PDB Sequence |
TSPRNWCIKM
75 VCNPWFECVS85 MLVILLNCVT95 LGMYQPCDDM105 DCLSDRCKIL115 QVFDDFIFIF 125 FAMEMVLKMV135 ALGIFGKKCY145 LGDTWNRLDF155 FIVMAGMVEY165 SLDLQNINLS 175 AIRTVRVLRP185 LKAINRVPSM195 RILVNLLLDT205 LPMLGNVLLL215 CFFVFFIFGI 225 IGVQLWAGLL235 RNRCFLEENF245 TIQGDVALPP255 YYQPEEDDEM265 PFICSLSGDN 275 GIMGCHEIPP285 LKCVNWNRYY323 NVCRTGSANP333 HKGAINFDNI343 GYAWIVIFQV 353 ITLEGWVEIM363 YYVMDAHSFY373 NFIYFILLII383 VGSFFMINLC393 LVVIATQFSE 403 TKQREHRLML413 RETRAKLRGI636 VDSKYFNRGI646 MMAILVNTVS656 MGIEHHEQPE 666 ELTNILEICN676 VVFTSMFALE686 MILKLAAFGL696 FDYLRNPYNI706 FDSIIVIISI 716 WEIVGQADGG726 LSVLRTFRLL736 RVLKLVRFMP746 ALRRQLVVLM756 KTMDNVATFC 766 MLLMLFIFIF776 SILGMHIFGC786 KFSLRTDTGD796 TVPDRKNFDS806 LLWAIVTVFQ 816 ILTQEDWNVV826 LYNGMASTSP836 WASLYFVALM846 TFGNYVLFNL856 LVAILVEGFQ 866 QTIIAHKLFD1173 YVVLAFIFLN1183 CITIALERPQ1193 IEAGSTERIF1203 LTVSNYIFTA 1213 IFVGEMTLKV1223 VSLGLYFGEQ1233 AYLRSSWNVL1243 DGFLVFVSII1253 DIVVSLASAG 1263 GAKILGVLRV1273 LRLLRTLRPL1283 RVISRAPGLK1293 LVVETLISSL1303 KPIGNIVLIC 1313 CAFFIIFGIL1323 GVQLFKGKFY1333 HCLGVDTRNI1343 TNRSDCMAAN1353 YRWVHHKYNF 1363 DNLGQALMSL1373 FVLASKDGWV1383 NIMYNGLDAV1393 AVDQQPVTNH1403 NPWMLLYFIS 1413 FLLIVSFFVL1423 NMFVGVVVEN1433 FHKCRQHQEA1443 EEARRREEKR1453 LRRLEKKRRK 1463 AQRLPYYATY1473 CHTRLLIHSM1483 CTSHYLDIFI1493 TFIICLNVVT1503 MSLEHYNQPT 1513 SLETALKYCN1523 YMFTTVFVLE1533 AVLKLVAFGL1543 RRFFKDRWNQ1553 LDLAIVLLSV 1563 MGITLEEIEI1573 NAALPINPTI1583 IRIMRVLRIA1593 RVLKLLKMAT1603 GMRALLDTVV 1613 QALPQVGNLG1623 LLFMLLFFIY1633 AALGVELFGK1643 LVCNDENPCE1653 GMSRHATFEN 1663 FGMAFLTLFQ1673 VSTGDNWNGI1683 MKDTLRDCTH1693 DERSCLSSLQ1703 FVSPLYFVSF 1713 VLTAQFVLIN1723 VVVAVLMKHL1733 DDSNK
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .3PE or .3PE2 or .3PE3 or :33PE;style chemicals stick;color identity;select .A:93 or .A:94 or .A:97 or .A:98 or .A:214 or .A:217 or .A:220 or .A:342 or .A:344 or .A:345 or .A:347 or .A:348 or .A:351 or .A:356 or .A:382 or .A:383 or .A:386 or .A:387 or .A:388 or .A:728 or .A:729 or .A:732 or .A:733 or .A:735 or .A:736 or .A:739 or .A:759 or .A:762 or .A:766 or .A:769 or .A:770 or .A:771 or .A:773 or .A:774 or .A:807 or .A:808 or .A:811 or .A:812 or .A:815 or .A:836 or .A:837 or .A:839 or .A:840 or .A:843 or .A:854 or .A:857 or .A:1299 or .A:1300 or .A:1303 or .A:1306 or .A:1310 or .A:1313 or .A:1314 or .A:1317 or .A:1319 or .A:1320 or .A:1323 or .A:1327 or .A:1374 or .A:1377 or .A:1378 or .A:1379 or .A:1404 or .A:1405 or .A:1406 or .A:1407 or .A:1408 or .A:1409 or .A:1410 or .A:1412 or .A:1413 or .A:1416 or .A:1417 or .A:1418 or .A:1419 or .A:1420 or .A:1422 or .A:1423 or .A:1425 or .A:1491 or .A:1494 or .A:1495 or .A:1498 or .A:1501 or .A:1598 or .A:1601 or .A:1602 or .A:1623 or .A:1626 or .A:1672 or .A:1675 or .A:1676 or .A:1677 or .A:1714 or .A:1715 or .A:1716 or .A:1718 or .A:1719 or .A:1721 or .A:1722; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
CYS93
4.567
VAL94
4.603
GLY97
4.428
MET98
4.179
LEU214
4.120
PHE217
3.914
PHE220
4.127
ASN342
3.821
GLY344
3.481
TYR345
3.989
TRP347
3.979
ILE348
3.575
PHE351
4.541
LEU356
3.673
ILE382
3.786
ILE383
4.303
SER386
4.484
PHE387
3.436
PHE388
4.018
SER728
4.668
VAL729
3.832
THR732
3.613
PHE733
4.558
LEU735
3.857
LEU736
4.042
LEU739
4.018
MET759
3.887
VAL762
4.413
CYS766
3.723
LEU769
4.687
MET770
3.617
LEU771
4.264
ILE773
4.346
PHE774
4.350
LEU807
3.933
LEU808
3.665
ILE811
3.589
VAL812
4.937
PHE815
4.243
PRO836
3.791
TRP837
3.457
SER839
3.262
LEU840
4.285
VAL843
3.634
PHE854
3.597
LEU857
4.069
LEU1299
3.844
ILE1300
4.292
LEU1303
4.127
ILE1306
4.257
VAL1310
4.420
CYS1313
4.139
CYS1314
4.340
PHE1317
4.224
ILE1319
4.391
PHE1320
4.252
LEU1323
3.813
LEU1327
4.283
PHE1374
3.667
ALA1377
2.954
SER1378
3.864
LYS1379
3.426
ASN1404
3.363
PRO1405
3.820
TRP1406
3.884
MET1407
4.186
LEU1408
3.609
LEU1409
3.650
TYR1410
4.046
ILE1412
3.533
SER1413
4.194
LEU1416
3.559
ILE1417
3.976
VAL1418
4.936
SER1419
4.162
PHE1420
3.629
VAL1422
3.344
LEU1423
3.647
MET1425
3.806
ILE1491
3.674
THR1494
4.117
PHE1495
3.764
CYS1498
3.665
VAL1501
4.180
LEU1598
4.081
MET1601
3.573
ALA1602
3.886
GLY1623
4.482
PHE1626
3.664
PHE1672
3.835
SER1675
3.822
THR1676
3.641
GLY1677
4.558
VAL1714
4.560
LEU1715
3.691
THR1716
4.485
GLN1718
3.416
PHE1719
3.611
LEU1721
3.719
ILE1722
3.811
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: Cholesterol hemisuccinate | Ligand Info | |||||
| Structure Description | CryoEM structure of human low-voltage activated T-type calcium channel CaV3.3 (apo) | PDB:7WLI | ||||
| Method | Electron microscopy | Resolution | 3.30 Å | Mutation | No | [1] |
| PDB Sequence |
TSPRNWCIKM
75 VCNPWFECVS85 MLVILLNCVT95 LGMYQPCDDM105 DCLSDRCKIL115 QVFDDFIFIF 125 FAMEMVLKMV135 ALGIFGKKCY145 LGDTWNRLDF155 FIVMAGMVEY165 SLDLQNINLS 175 AIRTVRVLRP185 LKAINRVPSM195 RILVNLLLDT205 LPMLGNVLLL215 CFFVFFIFGI 225 IGVQLWAGLL235 RNRCFLEENF245 TIQGDVALPP255 YYQPEEDDEM265 PFICSLSGDN 275 GIMGCHEIPP285 LKCVNWNRYY323 NVCRTGSANP333 HKGAINFDNI343 GYAWIVIFQV 353 ITLEGWVEIM363 YYVMDAHSFY373 NFIYFILLII383 VGSFFMINLC393 LVVIATQFSE 403 TKQREHRLML413 RETRAKLRGI636 VDSKYFNRGI646 MMAILVNTVS656 MGIEHHEQPE 666 ELTNILEICN676 VVFTSMFALE686 MILKLAAFGL696 FDYLRNPYNI706 FDSIIVIISI 716 WEIVGQADGG726 LSVLRTFRLL736 RVLKLVRFMP746 ALRRQLVVLM756 KTMDNVATFC 766 MLLMLFIFIF776 SILGMHIFGC786 KFSLRTDTGD796 TVPDRKNFDS806 LLWAIVTVFQ 816 ILTQEDWNVV826 LYNGMASTSP836 WASLYFVALM846 TFGNYVLFNL856 LVAILVEGFQ 866 QTIIAHKLFD1173 YVVLAFIFLN1183 CITIALERPQ1193 IEAGSTERIF1203 LTVSNYIFTA 1213 IFVGEMTLKV1223 VSLGLYFGEQ1233 AYLRSSWNVL1243 DGFLVFVSII1253 DIVVSLASAG 1263 GAKILGVLRV1273 LRLLRTLRPL1283 RVISRAPGLK1293 LVVETLISSL1303 KPIGNIVLIC 1313 CAFFIIFGIL1323 GVQLFKGKFY1333 HCLGVDTRNI1343 TNRSDCMAAN1353 YRWVHHKYNF 1363 DNLGQALMSL1373 FVLASKDGWV1383 NIMYNGLDAV1393 AVDQQPVTNH1403 NPWMLLYFIS 1413 FLLIVSFFVL1423 NMFVGVVVEN1433 FHKCRQHQEA1443 EEARRREEKR1453 LRRLEKKRRK 1463 AQRLPYYATY1473 CHTRLLIHSM1483 CTSHYLDIFI1493 TFIICLNVVT1503 MSLEHYNQPT 1513 SLETALKYCN1523 YMFTTVFVLE1533 AVLKLVAFGL1543 RRFFKDRWNQ1553 LDLAIVLLSV 1563 MGITLEEIEI1573 NAALPINPTI1583 IRIMRVLRIA1593 RVLKLLKMAT1603 GMRALLDTVV 1613 QALPQVGNLG1623 LLFMLLFFIY1633 AALGVELFGK1643 LVCNDENPCE1653 GMSRHATFEN 1663 FGMAFLTLFQ1673 VSTGDNWNGI1683 MKDTLRDCTH1693 DERSCLSSLQ1703 FVSPLYFVSF 1713 VLTAQFVLIN1723 VVVAVLMKHL1733 DDSNK
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .Y01 or .Y012 or .Y013 or :3Y01;style chemicals stick;color identity;select .A:175 or .A:222 or .A:223 or .A:226 or .A:230 or .A:275 or .A:370 or .A:371 or .A:372 or .A:373 or .A:374 or .A:375 or .A:376 or .A:377 or .A:379 or .A:380 or .A:383 or .A:384 or .A:654 or .A:655 or .A:658 or .A:659 or .A:661 or .A:776 or .A:779 or .A:783 or .A:787 or .A:834 or .A:835 or .A:837 or .A:838 or .A:840 or .A:841 or .A:844 or .A:848 or .A:1181 or .A:1184 or .A:1185 or .A:1188 or .A:1189 or .A:1191 or .A:1193 or .A:1314 or .A:1317 or .A:1318 or .A:1365 or .A:1366 or .A:1367 or .A:1368 or .A:1370 or .A:1371 or .A:1374 or .A:1585 or .A:1627 or .A:1631 or .A:1658 or .A:1663 or .A:1664 or .A:1665 or .A:1666 or .A:1668 or .A:1669 or .A:1672 or .A:1703 or .A:1704 or .A:1707 or .A:1708 or .A:1711 or .A:1715; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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SER175
4.521
ILE222
4.318
PHE223
3.503
ILE226
3.543
LEU230
3.616
ASN275
3.838
HIS370
3.582
SER371
3.025
PHE372
3.834
TYR373
3.132
ASN374
3.504
PHE375
3.469
ILE376
3.615
TYR377
3.579
ILE379
3.673
LEU380
3.979
ILE383
3.633
VAL384
3.657
THR654
4.101
VAL655
3.659
GLY658
3.448
ILE659
4.345
HIS661
3.387
PHE776
4.595
LEU779
3.886
ILE783
4.117
LYS787
4.987
THR834
3.587
SER835
3.545
TRP837
3.173
ALA838
3.550
LEU840
3.653
TYR841
3.260
ALA844
4.365
PHE848
4.716
PHE1181
3.652
CYS1184
3.623
ILE1185
3.653
ALA1188
3.729
LEU1189
3.625
ARG1191
3.366
GLN1193
3.980
CYS1314
3.940
PHE1317
4.136
ILE1318
4.773
ASN1365
3.452
LEU1366
3.525
GLY1367
3.364
GLN1368
4.066
LEU1370
4.469
MET1371
3.604
PHE1374
3.499
ARG1585
2.524
MET1627
3.545
PHE1631
3.862
HIS1658
4.534
ASN1663
3.663
PHE1664
3.432
GLY1665
3.984
MET1666
4.086
PHE1668
3.785
LEU1669
3.527
PHE1672
3.556
GLN1703
3.738
PHE1704
3.429
PRO1707
3.427
LEU1708
4.976
VAL1711
4.150
LEU1715
4.743
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: Otilonium | Ligand Info | |||||
| Structure Description | CryoEM structure of human low-voltage activated T-type calcium channel Cav3.3 in complex with Otilonium Bromide(OB) | PDB:7WLK | ||||
| Method | Electron microscopy | Resolution | 3.60 Å | Mutation | No | [1] |
| PDB Sequence |
TSPRNWCIKM
75 VCNPWFECVS85 MLVILLNCVT95 LGMYQPCDDM105 DCLSDRCKIL115 QVFDDFIFIF 125 FAMEMVLKMV135 ALGIFGKKCY145 LGDTWNRLDF155 FIVMAGMVEY165 SLDLQNINLS 175 AIRTVRVLRP185 LKAINRVPSM195 RILVNLLLDT205 LPMLGNVLLL215 CFFVFFIFGI 225 IGVQLWAGLL235 RNRCFLEENF245 TIQGDVALPP255 YYQPEEDDEM265 PFICSLSGDN 275 GIMGCHEIPP285 LKCVNWNRYY323 NVCRTGSANP333 HKGAINFDNI343 GYAWIVIFQV 353 ITLEGWVEIM363 YYVMDAHSFY373 NFIYFILLII383 VGSFFMINLC393 LVVIATQFSE 403 TKQREHRLML413 RETRAKLRGI636 VDSKYFNRGI646 MMAILVNTVS656 MGIEHHEQPE 666 ELTNILEICN676 VVFTSMFALE686 MILKLAAFGL696 FDYLRNPYNI706 FDSIIVIISI 716 WEIVGQADGG726 LSVLRTFRLL736 RVLKLVRFMP746 ALRRQLVVLM756 KTMDNVATFC 766 MLLMLFIFIF776 SILGMHIFGC786 KFSLRTDTGD796 TVPDRKNFDS806 LLWAIVTVFQ 816 ILTQEDWNVV826 LYNGMASTSP836 WASLYFVALM846 TFGNYVLFNL856 LVAILVEGFQ 866 QTIIAHKLFD1173 YVVLAFIFLN1183 CITIALERPQ1193 IEAGSTERIF1203 LTVSNYIFTA 1213 IFVGEMTLKV1223 VSLGLYFGEQ1233 AYLRSSWNVL1243 DGFLVFVSII1253 DIVVSLASAG 1263 GAKILGVLRV1273 LRLLRTLRPL1283 RVISRAPGLK1293 LVVETLISSL1303 KPIGNIVLIC 1313 CAFFIIFGIL1323 GVQLFKGKFY1333 HCLGVDTRNI1343 TNRSDCMAAN1353 YRWVHHKYNF 1363 DNLGQALMSL1373 FVLASKDGWV1383 NIMYNGLDAV1393 AVDQQPVTNH1403 NPWMLLYFIS 1413 FLLIVSFFVL1423 NMFVGVVVEN1433 FHKCRQHQEA1443 EEARRREEKR1453 LRRLEKKRRK 1463 AQRLPYYATY1473 CHTRLLIHSM1483 CTSHYLDIFI1493 TFIICLNVVT1503 MSLEHYNQPT 1513 SLETALKYCN1523 YMFTTVFVLE1533 AVLKLVAFGL1543 RRFFKDRWNQ1553 LDLAIVLLSV 1563 MGITLEEIEI1573 NAALPINPTI1583 IRIMRVLRIA1593 RVLKLLKMAT1603 GMRALLDTVV 1613 QALPQVGNLG1623 LLFMLLFFIY1633 AALGVELFGK1643 LVCNDENPCE1653 GMSRHATFEN 1663 FGMAFLTLFQ1673 VSTGDNWNGI1683 MKDTLRDCTH1693 DERSCLSSLQ1703 FVSPLYFVSF 1713 VLTAQFVLIN1723 VVVAVLMKHL1733 DDSNK
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .7TB or .7TB2 or .7TB3 or :37TB;style chemicals stick;color identity;select .A:390 or .A:391 or .A:394 or .A:759 or .A:762 or .A:766 or .A:769 or .A:815 or .A:818 or .A:819 or .A:820 or .A:850 or .A:854 or .A:857 or .A:1379 or .A:1416 or .A:1417 or .A:1419 or .A:1420 or .A:1422 or .A:1426 or .A:1718 or .A:1722 or .A:1725; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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ILE390
4.712
ASN391
3.920
LEU394
4.604
MET759
3.606
VAL762
4.041
CYS766
3.779
LEU769
4.589
PHE815
3.170
LEU818
3.560
THR819
3.469
GLN820
3.188
ASN850
3.080
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Structure, gating, and pharmacology of human Ca(V)3.3 channel. Nat Commun. 2022 Apr 19;13(1):2084. | ||||
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