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 T60213 Target Info
Target Name Bone morphogenetic protein receptor (BMPR2)
Synonyms PPH1; Bone morphogenetic protein receptor type-2; Bone morphogenetic protein receptor type II; BMPR-II; BMPR-2; BMP type-2 receptor; BMP type II receptor
Target Type Literature-reported Target
Gene Name BMPR2
Biochemical Class Kinase
UniProt ID
BMPR2_HUMAN
Ligand General Information  Top
Ligand Name S-(Dimethylarsenic)Cysteine Ligand Info
Canonical SMILES C[As](C)SCC(C(=O)O)N
InChI 1S/C5H12AsNO2S/c1-6(2)10-3-4(7)5(8)9/h4H,3,7H2,1-2H3,(H,8,9)/t4-/m0/s1
InChIKey UKLXSOVDMSQHMM-BYPYZUCNSA-N
PubChem Compound ID 17753880
Drug Binding Sites of Target  Top
PDB ID: 6UNP      Crystal structure of the kinase domain of BMPR2-D485G
Method X-ray diffraction Resolution 2.30 Å Mutation Yes [1]
PDB Sequence
DLDNLKLLEL
208
IGRGRYGAVY
218
KGSLDERPVA
228
VKVFSFANRQ
238
NFINEKNIYR
248

VPLMEHDNIA
258
RFIVGDERVT
268
ADGRMEYLLV
278
MEYYPNGSLK
289
YLSLHTSDWV
299

SSCRLAHSVT
309
RGLAYLHTEL
319
PRGDHYKPAI
329
SHRDLNSRNV
339
LVKNDGTCVI
349

SDFGLSMRLT
359
GNRLVRPEVG
378
TIRYMAPEVL
388
EGAVNLRDES
399
ALKQVDMYAL
409

GLIYWEIFMR
419
CTDLFPGESV
429
PEYQMAFQTE
439
VGNHPTFEDM
449
QVLVSREKQR
459

PKFPEAWKEN
469
SLAVRSLKET
479
IEDCWGQDAE
489
ARLTAQAEER
500
MAELMMIWE
Residue
Distance (Å)
SER286
3.148
LEU287
1.335
LYS289
1.320
TYR290
3.274
LEU291
3.393
SER292
2.992
SER336
2.895
ARG337
3.739
VAL339
4.998
MET356
4.763
ARG357
4.523
LEU358
4.053
VAL364
4.327
PRO366
4.348
ASN393
4.074
LEU394
3.339
ARG395
3.368
Residue
Distance (Å)
ASP396
1.319
GLU398
1.331
SER399
3.344
ALA400
3.356
LEU401
3.033
LYS402
4.968
TYR432
3.655
MET434
4.647
LEU492
3.886
THR493
3.217
ALA494
3.260
GLN495
1.328
ALA497
1.334
GLU498
3.201
GLU499
3.241
ARG500
2.714
MET501
4.809
PDB ID: 3G2F      Crystal structure of the kinase domain of bone morphogenetic protein receptor type II (BMPR2) at 2.35 A resolution
Method X-ray diffraction Resolution 2.35 Å Mutation No [2]
PDB Sequence
SLDLDNLKLL
206
ELIGRGRYGA
216
VYKGSLDERP
226
VAVKVFSFAN
236
RQNFINEKNI
246

YRVPLMEHDN
256
IARFIVGDER
266
VTADGRMEYL
276
LVMEYYPNGS
286
LKYLSLHTSD
297

WVSSCRLAHS
307
VTRGLAYLHT
317
ELPRGDHYKP
327
AISHRDLNSR
337
NVLVKNDGTC
347

VISDFGLSMR
357
LTGNRLVISE
376
VGTIRYMAPE
386
VLEGAVNLRD
396
ESALKQVDMY
407

ALGLIYWEIF
417
MRCTDLFPGE
427
SVPEYQMAFQ
437
TEVGNHPTFE
447
DMQVLVSREK
457

QRPKFPEAWK
467
ENSLAVRSLK
477
ETIEDCWDQD
487
AEARLTAQAE
498
ERMAELMMIW
508

ER
Residue
Distance (Å)
SER286
3.230
LEU287
1.325
LYS289
1.321
TYR290
3.371
LEU291
3.571
SER292
3.129
SER336
3.088
ARG337
3.992
VAL339
4.809
MET356
4.639
ARG357
4.400
LEU358
4.005
LEU363
4.277
VAL364
4.478
ASN393
4.444
LEU394
3.544
Residue
Distance (Å)
ARG395
3.567
ASP396
1.334
GLU398
1.329
SER399
3.422
ALA400
3.429
LEU401
3.100
TYR432
3.616
MET434
4.916
LEU492
3.912
THR493
3.053
ALA494
3.282
GLN495
1.333
ALA497
1.332
GLU498
3.289
GLU499
3.121
ARG500
3.001
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 Structural consequences of BMPR2 kinase domain mutations causing pulmonary arterial hypertension. Sci Rep. 2019 Dec 4;9(1):18351.

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