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 T86573 Target Info
Target Name HUMAN inosine-5'-monophosphate dehydrogenase 2 (IMPDH2)
Synonyms IMPDH-II; IMPDH 2; IMPD2; IMPD 2; IMP dehydrogenase 2
Gene Name IMPDH2
Biochemical Class CH-OH donor oxidoreductase
UniProt ID
IMDH2_HUMAN
Ligand General Information  Top
Ligand Name 6-Chloropurine Riboside, 5'-Monophosphate Ligand Info
Canonical SMILES C1=[N+](C2=C(N1)C(=NC=N2)Cl)C3C(C(C(O3)COP(=O)(O)O)O)O
InChI 1S/C10H12ClN4O7P/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(22-10)1-21-23(18,19)20/h2-4,6-7,10,16-17H,1H2,(H2,18,19,20)/p+1/t4-,6-,7-,10-/m1/s1
InChIKey ALOBOMYIOYNCBS-KQYNXXCUSA-O
PubChem Compound ID 17753915
Drug Binding Sites of Target  Top
PDB ID: 1B3O      TERNARY COMPLEX OF HUMAN TYPE-II INOSINE MONOPHOSPHATE DEHYDROGENASE WITH 6-CL-IMP AND SELENAZOLE ADENINE DINUCLEOTIDE
Method X-ray diffraction Resolution 2.90 Å Mutation No [1]
PDB Sequence
TSYVPDDGLT
19
AQQLFNCGDG
29
LTYNDFLILP
39
GYIDFTADQV
49
DLTSALTKKI
59

TLKTPLVSSP
69
MDTVTEAGMA
79
IAMALTGGIG
89
FIHHNCTPEF
99
QANEVRKVKK
109

DYPLASKDAK
241
KQLLCGAAIG
251
THEDDKYRLD
261
LLAQAGVDVV
271
VLDSSQGNSI
281

FQINMIKYIK
291
DKYPNLQVIG
301
GNVVTAAQAK
311
NLIDAGVDAL
321
RVGMGSRPQA
344

TAVYKVSEYA
354
RRFGVPVIAD
364
GGIQNVGHIA
374
KALALGASTV
384
MMGSLLAATT
394

EAPGEYDKGS
452
IHKFVPYLIA
462
GIQHSCQDIG
472
AKSLTQVRAM
482
MYSGELKFEK
492

RTSSAQV
Residue
Distance (Å)
SER68
3.126
PRO69
4.689
MET70
3.748
ASN303
3.834
ARG322
2.796
SER327
3.693
ASP364
2.477
GLY365
3.800
Residue
Distance (Å)
GLY366
2.972
ILE367
4.621
MET385
3.567
MET386
3.940
GLY387
2.957
SER388
2.420
LEU389
4.769
PDB ID: 1NFB      Ternary complex of the human type II Inosine Monophosphate Dedhydrogenase with 6Cl-IMP and NAD
Method X-ray diffraction Resolution 2.90 Å Mutation No [2]
PDB Sequence
TSYVPDDGLT
19
AQQLFNCGDG
29
LTYNDFLILP
39
GYIDFTADQV
49
DLTSALTKKI
59

TLKTPLVSSP
69
MDTVTEAGMA
79
IAMALTGGIG
89
FIHHNCTPEF
99
QANEVRKVKK
109

YEQGFITDPV
119
VLSPGIPITD
146
TGRMGSAPAG
191
ITLKEANEIL
201
QRSKKGKLPI
211

VNEDDEVAII
222
ANRDYPLASK
238
DAKKQLLCGA
248
AIGTHEDDKY
258
RLDLLAQAGV
268

DVVVLDSSQG
278
NSIFQINMIK
288
YIKDKYPNLQ
298
VIGGNVVTAA
308
QAKNLIDAGV
318

DALRVGMGSG
328
SICITQEVLA
338
CGRPQATAVY
348
KVSEYARRFG
358
VPVIADGGIQ
368

NVGHIAKALA
378
LGASTVMMGS
388
LLAATTEAPG
398
EYFFSDGIRL
408
KKYRGMDKGS
452

IHKFVPYLIA
462
GIQHSCQDIG
472
AKSLTQVRAM
482
MYSGELKFEK
492
RTSSAQ
Residue
Distance (Å)
SER68
2.788
PRO69
4.824
MET70
3.398
ASN303
4.169
ARG322
3.746
SER327
3.768
GLY328
2.995
SER329
2.879
ILE330
3.678
CYS331
1.854
ILE332
4.578
Residue
Distance (Å)
GLU335
3.614
ASP364
2.397
GLY365
3.207
GLY366
2.563
ILE367
3.757
MET385
3.797
MET386
4.093
GLY387
2.962
SER388
2.873
LEU389
4.521
TYR411
3.443
References  Top
REF 1 Crystal structure of human type II inosine monophosphate dehydrogenase: implications for ligand binding and drug design. Proc Natl Acad Sci U S A. 1999 Mar 30;96(7):3531-6.
REF 2 The Conformation of NAD Bound to Human Inosine Monophosphate Dehydrogenase Type II

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