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 3-[6-Amino-5-(3,4,5-Trimethoxyphenyl)pyridin-3-Yl]phenol Ligand Info
Canonical SMILES COC1=CC(=CC(=C1OC)OC)C2=C(N=CC(=C2)C3=CC(=CC=C3)O)N
InChI 1S/C20H20N2O4/c1-24-17-9-13(10-18(25-2)19(17)26-3)16-8-14(11-22-20(16)21)12-5-4-6-15(23)7-12/h4-11,23H,1-3H3,(H2,21,22)
InChIKey CJLMANFTWLNAKC-UHFFFAOYSA-N
PubChem Compound ID 46173038
Drug Binding Sites of Target  Top
PDB ID: 6EIX      Crystal structure of the kinase domain of the Q207E mutant of ACVR1 (ALK2) in complex with a 2-aminopyridine inhibitor K02288
Method X-ray diffraction Resolution 2.30 Å Mutation Yes [1]
PDB Sequence
SGSGLPFLVQ
201
RTVAREITLL
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

KKTLTKIDNS
501
LD
Residue
Distance (Å)
VAL214
3.800
VAL222
3.837
ALA233
3.170
VAL234
4.118
LYS235
3.450
GLU248
3.923
LEU263
3.604
LEU281
3.487
ILE282
4.733
THR283
3.043
HIS284
2.751
Residue
Distance (Å)
TYR285
3.795
HIS286
3.043
GLU287
4.790
GLY289
3.493
SER290
3.292
ASP293
2.652
LYS340
3.357
ASN341
3.468
LEU343
3.599
ALA353
3.854
ASP354
3.854
PDB ID: 3MTF      Crystal structure of the ACVR1 kinase in complex with a 2-aminopyridine inhibitor
Method X-ray diffraction Resolution 2.15 Å Mutation Yes [2]
PDB Sequence
TVARDITLLE
212
CVGKGRYGEV
222
WRGSWQGENV
232
AVKIFSSRDE
242
KSWFRETELY
252

NTVMLRHENI
262
LGFIASDMTS
272
RHSSTQLWLI
282
THYHEMGSLY
292
DYLQLTTLDT
302

VSCLRIVLSI
312
ASGLAHLHIE
322
IFGTQGKPAI
332
AHRDLKSKNI
342
LVKKNGQCCI
352

ADLGLAVMHS
362
QSTNQLDVGN
372
NPRVGTKRYM
382
APEVLDETIQ
392
VDCFDSYKRV
402

DIWAFGLVLW
412
EVARRMVSNG
422
IVEDYKPPFY
432
DVVPNDPSFE
442
DMRKVVCVDQ
452

QRPNIPNRWF
462
SDPTLTSLAK
472
LMKECWYQNP
482
SARLTALRIK
492
KTLTKI
Residue
Distance (Å)
VAL214
3.785
VAL222
3.855
ALA233
3.433
VAL234
3.916
LYS235
3.326
GLU248
3.690
LEU263
3.596
LEU281
3.453
ILE282
4.837
THR283
3.200
HIS284
2.886
Residue
Distance (Å)
TYR285
3.529
HIS286
2.919
GLU287
4.837
GLY289
3.496
SER290
3.329
ASP293
2.724
LYS340
3.224
ASN341
3.598
LEU343
3.300
ALA353
3.870
ASP354
3.467
References  Top
REF 1 Crystal structure of the kinase domain of the Q207E mutant of ACVR1 (ALK2) in complex with K02288
REF 2 A new class of small molecule inhibitor of BMP signaling. PLoS One. 2013 Apr 30;8(4):e62721.

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