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 T12091 Target Info
Target Name Activin receptor-like kinase 2 (ALK-2)
Synonyms TSR-I; TGF-B superfamily receptor type I; Serine/threonine-protein kinase receptor R1; SKR1; Activin receptor type-1; Activin receptor type I; ACVRLK2; ACTR-I
Target Type Clinical trial Target
Gene Name ACVR1
Biochemical Class Kinase
UniProt ID
ACVR1_HUMAN
Ligand General Information  Top
Ligand Name 4-(6-(4-(Piperazin-1-yl)phenyl)pyrazolo[1,5-a]pyrimidin-3-yl)quinoline Ligand Info
Canonical SMILES C1CN(CCN1)C2=CC=C(C=C2)C3=CN4C(=C(C=N4)C5=CC=NC6=CC=CC=C56)N=C3
InChI 1S/C25H22N6/c1-2-4-24-22(3-1)21(9-10-27-24)23-16-29-31-17-19(15-28-25(23)31)18-5-7-20(8-6-18)30-13-11-26-12-14-30/h1-10,15-17,26H,11-14H2
InChIKey CDOVNWNANFFLFJ-UHFFFAOYSA-N
PubChem Compound ID 25195294
Drug Binding Sites of Target  Top
PDB ID: 6UNS      Kinase domain of ALK2-K492A/K493A with LDN-193189
Method X-ray diffraction Resolution 2.30 Å Mutation Yes [1]
PDB Sequence
VARQITLLEC
213
VGKGRYGEVW
223
RGSWQGENVA
233
VKIFSSRDEK
243
SWFRETELYN
253

TVMLRHENIL
263
GFIASDMTSR
273
STQLWLITHY
285
HEMGSLYDYL
295
QLTTLDTVSC
305

LRIVLSIASG
315
LAHLHIEIQG
328
KPAIAHRDLK
338
SKNILVKKNG
348
QCCIADLGLA
358

VMHSQSTNQL
368
DVGNNPRVGT
378
KRYMAPEVLD
388
ETIQVDCFDS
398
YKRVDIWAFG
408

LVLWEVARRM
418
VSNGIVEDYK
428
PPFYDVVPND
438
PSFEDMRKVV
448
CVDQQRPNIP
458

NRWFSDPTLT
468
SLAKLMKECW
478
YQNPSARLTA
488
LRIAATLT
Residue
Distance (Å)
VAL214
3.717
VAL222
3.735
ALA233
3.448
LYS235
3.432
GLU248
4.990
LEU263
3.593
LEU281
4.903
THR283
3.349
HIS284
3.351
TYR285
3.290
HIS286
3.209
Residue
Distance (Å)
GLU287
3.249
MET288
3.724
GLY289
3.461
SER290
4.363
ASP293
3.628
LEU297
4.052
LYS340
3.563
ASN341
3.428
LEU343
3.481
ALA353
3.659
ASP354
4.108
PDB ID: 3Q4U      Crystal structure of the ACVR1 kinase domain in complex with LDN-193189
Method X-ray diffraction Resolution 1.82 Å Mutation Yes [2]
PDB Sequence
RTVARDITLL
211
ECVGKGRYGE
221
VWRGSWQGEN
231
VAVKIFSSRD
241
EKSWFRETEL
251

YNTVMLRHEN
261
ILGFIASDMT
271
SRHSSTQLWL
281
ITHYHEMGSL
291
YDYLQLTTLD
301

TVSCLRIVLS
311
IASGLAHLHI
321
EIFGTQGKPA
331
IAHRDLKSKN
341
ILVKKNGQCC
351

IADLGLAVMH
361
SQSTNQLDVG
371
NNPRVGTKRY
381
MAPEVLDETI
391
QVDCFDSYKR
401

VDIWAFGLVL
411
WEVARRMVSN
421
GIVEDYKPPF
431
YDVVPNDPSF
441
EDMRKVVCVD
451

QQRPNIPNRW
461
FSDPTLTSLA
471
KLMKECWYQN
481
PSARLTALRI
491
KKTLTKID
Residue
Distance (Å)
VAL214
3.635
VAL222
3.493
ALA233
3.538
LYS235
3.763
LEU263
3.473
LEU281
4.768
THR283
3.236
HIS284
3.558
TYR285
3.519
HIS286
3.188
Residue
Distance (Å)
GLU287
3.348
MET288
4.335
GLY289
3.472
SER290
4.385
ASP293
3.499
LYS340
3.571
ASN341
3.565
LEU343
3.679
ALA353
3.772
ASP354
4.128
References  Top
REF 1 Structural basis for ALK2/BMPR2 receptor complex signaling through kinase domain oligomerization. Nat Commun. 2021 Aug 16;12(1):4950.
REF 2 A new class of small molecule inhibitor of BMP signaling. PLoS One. 2013 Apr 30;8(4):e62721.

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