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 T40787 Target Info
Target Name S-methyl-5'-thioadenosine phosphorylase (MTAP)
Synonyms Methylthioadenosine phosphorylase; MTAPase; MTA phosphorylase; MSAP; 5'-methylthioadenosine phosphorylase
Target Type Literature-reported Target
Gene Name MTAP
Biochemical Class Glycosyltransferases
UniProt ID
MTAP_HUMAN
Ligand General Information  Top
Ligand Name 5'-Deoxy-5'-(Methylthio)-Tubercidin Ligand Info
Canonical SMILES CSCC1C(C(C(O1)N2C=CC3=C(N=CN=C32)N)O)O
InChI 1S/C12H16N4O3S/c1-20-4-7-8(17)9(18)12(19-7)16-3-2-6-10(13)14-5-15-11(6)16/h2-3,5,7-9,12,17-18H,4H2,1H3,(H2,13,14,15)/t7-,8-,9-,12-/m1/s1
InChIKey WBPLMFVTQMIPLW-MFYTUXHUSA-N
PubChem Compound ID 188350
Drug Binding Sites of Target  Top
PDB ID: 1SD2      STRUCTURE OF HUMAN 5'-DEOXY-5'-METHYLTHIOADENOSINE PHOSPHORYLASE COMPLEXED WITH 5'-METHYLTHIOTUBERCIDIN
Method X-ray diffraction Resolution 2.10 Å Mutation No [1]
PDB Sequence
AVKIGIIGGT
18
GLDDPEILEG
28
RTEKYVDTPF
38
GKPSDALILG
48
KIKNVDCVLL
58

ARHGRQHTIM
68
PSKVNYQANI
78
WALKEEGCTH
88
VIVTTACGSL
98
REEIQPGDIV
108

IIDQFIDRTT
118
MRPQSFYDGG
134
VCHIPMAEPF
144
CPKTREVLIE
154
TAKKLGLRCH
164

SKGTMVTIEG
174
PRFSSRAESF
184
MFRTWGADVI
194
NMTTVPEVVL
204
AKEAGICYAS
214

IAMATDYDCW
224
AVSVDRVLKT
239
LKENANKAKS
249
LLLTTIPQIG
259
STEWSETLHN
269

LKNMAQFSVL
279
LP
Residue
Distance (Å)
THR18
4.093
HIS61
3.817
HIS65
4.673
PRO69
3.303
THR93
4.546
ALA94
3.250
CYS95
3.523
GLY96
3.521
ILE172
3.954
PHE177
3.665
ILE194
3.688
Residue
Distance (Å)
ASN195
3.474
MET196
2.907
THR197
4.037
THR219
3.537
ASP220
3.281
ASP222
2.980
VAL231
3.658
VAL233
4.368
VAL236
3.819
LEU237
4.396
PDB ID: 5TC7      Crystal structure of human 5'-deoxy-5'-methylthioadenosine phosphorylase in complex with 5'-methylthiotubercidin at 1.75 angstrom
Method X-ray diffraction Resolution 1.75 Å Mutation No [2]
PDB Sequence
AVKIGIIGGT
18
GLDDPEILEG
28
RTEKYVDTPF
38
GKPSDALILG
48
KIKNVDCVLL
58

ARHGRQHTIM
68
PSKVNYQANI
78
WALKEEGCTH
88
VIVTTACGSL
98
REEIQPGDIV
108

IIDQFIDRTT
118
MRPQSFYDGS
128
HSCARGVCHI
138
PMAEPFCPKT
148
REVLIETAKK
158

LGLRCHSKGT
168
MVTIEGPRFS
178
SRAESFMFRT
188
WGADVINMTT
198
VPEVVLAKEA
208

GICYASIAMA
218
TDYDCWKEHE
228
EAVSVDRVLK
238
TLKENANKAK
248
SLLLTTIPQI
258

GSTEWSETLH
268
NLKNMAQFSV
278
LLP
Residue
Distance (Å)
THR18
3.938
HIS61
3.867
HIS65
4.814
PRO69
3.533
THR93
4.680
ALA94
3.197
CYS95
3.566
GLY96
3.486
ILE172
3.807
PHE177
3.665
ILE194
3.727
Residue
Distance (Å)
ASN195
3.467
MET196
2.868
THR197
3.951
THR219
3.647
ASP220
3.092
ASP222
2.976
VAL231
3.976
VAL233
4.507
VAL236
3.773
LEU237
4.567
References  Top
REF 1 Structural comparison of MTA phosphorylase and MTA/AdoHcy nucleosidase explains substrate preferences and identifies regions exploitable for inhibitor design. Biochemistry. 2004 May 11;43(18):5159-69.
REF 2 TBA

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