Binding Site Information of Target

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Target General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T17448 Target Info
Target Name Histamine N-methyltransferase (HNMT)
Synonyms Histamine-N-methyltransferase; HNMT; HMT
Target Type Successful Target
Gene Name HNMT
Biochemical Class Methyltransferase
UniProt ID
HNMT_HUMAN
Drug Binding Sites of Target  Top
Ligand Name: Diphenhydramine Ligand Info
Structure Description Histamine Methyltransferase Complexed with the Antihistamine Drug Diphenhydramine PDB:2AOT
Method X-ray diffraction Resolution 1.90 Å Mutation Yes [1]
PDB Sequence
> Chain A
MRSLFSDHGK
14
YVESFRRFLN
24
HSTEHQCMQE
34
FMDKKLPGII
44
GRIGDTKSEI
54

KILSIGGGAG
64
EIDLQILSKV
74
QAQYPGVCIN
84
NEVVEPSAEQ
94
IAKYKELVAK
104

TSNLENVKFA
114
WHKETSSEYQ
124
SRMLEKKELQ
134
KWDFIHMIQM
144
LYYVKDIPAT
154

LKFFHSLLGT
164
NAKMLIIVVS
174
GSSGWDKLWK
184
KYGSRFPQDD
194
LCQYITSDDL
204

TQMLDNLGLK
214
YEYDLLSTMD
225
ISDCFIDGNE
235
NGDLLWDFLT
245
ETNFNATAPP
256

DLRAELGKDL
266
QEPEFSAKKE
276
GKVLFNNTLS
286
FIVIEA
> Chain B
MRSLFSDHGK
14
YVESFRRFLN
24
HSTEHQCMQE
34
FMDKKLPGII
44
GRIGDTKSEI
54

KILSIGGGAG
64
EIDLQILSKV
74
QAQYPGVINN
85
EVVEPSAEQI
95
AKYKELVAKT
105

SNLENVKFAW
115
HKETSSEYQS
125
RMLEKKELQK
135
WDFIHMIQML
145
YYVKDIPATL
155

KFFHSLLGTN
165
AKMLIIVVSG
175
SSGWDKLWKK
185
YGSRFPQDDL
195
CQYITSDDLT
205

QMLDNLGLKY
215
ECYDLLSTMD
225
ISDCFIDGNE
235
NGDLLWDFLT
245
ETNFNATAPP
256

DLRAELGKDL
266
QEPEFSAKKE
276
GKVLFNNTLS
286
FIVIEA
Residue
Distance (Å)
LEU8[A]
4.476
PHE9[A]
3.923
PHE19[A]
4.015
PHE22[A]
3.718
GLU28[A]
4.600
GLN143[A]
3.702
TYR146[A]
3.522
TYR147[A]
3.516
VAL173[A]
3.892
TRP179[A]
3.598
TRP183[A]
3.539
CYS196[A]
3.747
GLN197[A]
3.575
TYR198[A]
3.466
PHE243[A]
3.470
GLU246[A]
4.369
ASN283[A]
4.731
LEU8[B]
4.123
Residue
Distance (Å)
PHE9[B]
3.722
TYR15[B]
3.406
PHE19[B]
4.371
PHE22[B]
3.602
GLU28[B]
4.958
GLN143[B]
3.905
TYR146[B]
3.530
TYR147[B]
3.589
VAL173[B]
3.909
TRP179[B]
3.473
TRP183[B]
3.550
CYS196[B]
3.160
GLN197[B]
3.423
TYR198[B]
3.320
ILE199[B]
4.885
PHE243[B]
3.485
GLU246[B]
3.108
ASN283[B]
4.674
Ligand Name: Ergotidine Ligand Info
Structure Description Crystal Structure Analysis of Human Histamine Methyltransferase (Thr105 Polymorphic Variant) Complexed with AdoHcy and Histamine PDB:1JQD
Method X-ray diffraction Resolution 2.28 Å Mutation No [2]
PDB Sequence
MRSLFHGKYV
16
ESFRRFLNHS
26
TEHQCMQEFM
36
DKKLPGIIGR
46
IGDTKSEIKI
56

LSIGGGAGEI
66
DLQILSKVQA
76
QYPGVCINNE
86
VVEPSAEQIA
96
KYKELVAKTS
106

NLENVKFAWH
116
KETSSEYQSR
126
MLEKKELQKW
136
DFIHMIQMLY
146
YVKDIPATLK
156

FFHSLLGTNA
166
KMLIIVVSGS
176
SGWDKLWKKY
186
GSRFPQDDLC
196
QYITSDDLTQ
206

MLDNLGLKYE
216
CYDLLSTMDI
226
SDCFIDGNEN
236
GDLLWDFLTE
246
TCNFNATAPP
256

DLRAELGKDL
266
QEPEFSAKKE
276
GKVLFNNTLS
286
FIVIEA
Residue
Distance (Å)
PHE22
3.324
GLU28
2.693
GLN143
3.006
TYR146
4.108
TYR147
4.501
VAL173
3.436
Residue
Distance (Å)
TRP179
3.862
TRP183
3.714
PHE243
4.205
ASN283
2.637
LEU285
4.037
Ligand Name: Amodiaquine Ligand Info
Structure Description Histamine Methyltransferase Complexed with the Antimalarial Drug Amodiaquine PDB:2AOU
Method X-ray diffraction Resolution 2.30 Å Mutation Yes [1]
PDB Sequence
> Chain A
MRSLFSDHGK
14
YVESFRRFLN
24
HSTEHQCMQE
34
FMDKKLPGII
44
GRIGDTKSEI
54

KILSIGGGAG
64
EIDLQILSKV
74
QAQYPGVCIN
84
NEVVEPSAEQ
94
IAKYKELVAK
104

TSNLENVKFA
114
WHKETSSEYQ
124
SRMLEKKELQ
134
KWDFIHMIQM
144
LYYVKDIPAT
154

LKFFHSLLGT
164
NAKMLIIVVS
174
GSSGWDKLWK
184
KYGSRFPQDD
194
LCQYITSDDL
204

TQMLDNLGLK
214
YEYDLLSTMD
225
ISDCFIDGNE
235
NGDLLWDFLT
245
ETNFNATAPP
256

DLRAELGKDL
266
QEPEFSAKKE
276
GKVLFNNTLS
286
FIVIEA
> Chain B
SMRSLFSDHG
13
KYVESFRRFL
23
NHSTEHQCMQ
33
EFMDKKLPGI
43
IGRIGDTKSE
53

IKILSIGGGA
63
GEIDLQILSK
73
VQAQYPGVIN
84
NEVVEPSAEQ
94
IAKYKELVAK
104

TSNLENVKFA
114
WHKETSSEYQ
124
SRMLEKKELQ
134
KWDFIHMIQM
144
LYYVKDIPAT
154

LKFFHSLLGT
164
NAKMLIIVVS
174
GSSGWDKLWK
184
KYGSRFPQDD
194
LCQYITSDDL
204

TQMLDNLGLK
214
YECYDLLSTM
224
DISDCFIDGN
234
ENGDLLWDFL
244
TETCNFNATA
254

PPDLRAELGK
264
DLQEPEFSAK
274
KEGKVLFNNT
284
LSFIVIEA
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CQA or .CQA2 or .CQA3 or :3CQA;style chemicals stick;color identity;select .A:6 or .A:7 or .A:8 or .A:15 or .A:16 or .A:18 or .A:19 or .A:22 or .A:28 or .A:94 or .A:97 or .A:143 or .A:146 or .A:147 or .A:173 or .A:179 or .A:180 or .A:183 or .A:184 or .A:186 or .A:187 or .A:188 or .A:190 or .A:191 or .A:192 or .A:193 or .A:196 or .A:197 or .A:198 or .A:200 or .A:203 or .A:243 or .A:245 or .A:246 or .A:247 or .A:283 or .B:5 or .B:6 or .B:7 or .B:8 or .B:15 or .B:16 or .B:19 or .B:22 or .B:28 or .B:91 or .B:94 or .B:143 or .B:146 or .B:147 or .B:173 or .B:179 or .B:183 or .B:184 or .B:187 or .B:188 or .B:190 or .B:191 or .B:193 or .B:198 or .B:243 or .B:245 or .B:246 or .B:247 or .B:283; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ARG6[A]
4.418
SER7[A]
3.704
LEU8[A]
4.579
TYR15[A]
2.892
VAL16[A]
4.035
SER18[A]
4.952
PHE19[A]
3.307
PHE22[A]
4.127
GLU28[A]
3.352
GLN94[A]
3.303
LYS97[A]
4.901
GLN143[A]
3.220
TYR146[A]
3.576
TYR147[A]
3.309
VAL173[A]
3.398
TRP179[A]
3.248
ASP180[A]
3.388
TRP183[A]
3.303
LYS184[A]
3.538
TYR186[A]
4.585
GLY187[A]
3.321
SER188[A]
4.382
PHE190[A]
3.395
PRO191[A]
3.090
GLN192[A]
4.710
ASP193[A]
3.714
CYS196[A]
3.318
GLN197[A]
4.948
TYR198[A]
3.295
THR200[A]
4.678
ASP203[A]
4.807
PHE243[A]
3.637
THR245[A]
3.184
Residue
Distance (Å)
GLU246[A]
3.081
THR247[A]
3.657
ASN283[A]
4.670
MET5[B]
4.115
ARG6[B]
3.419
SER7[B]
3.248
LEU8[B]
4.887
TYR15[B]
2.574
VAL16[B]
4.148
PHE19[B]
3.233
PHE22[B]
3.884
GLU28[B]
3.410
SER91[B]
3.692
GLN94[B]
3.386
GLN143[B]
3.317
TYR146[B]
3.548
TYR147[B]
3.735
VAL173[B]
3.572
TRP179[B]
3.176
TRP183[B]
3.435
LYS184[B]
4.657
GLY187[B]
3.420
SER188[B]
4.485
PHE190[B]
3.368
PRO191[B]
3.100
ASP193[B]
3.561
TYR198[B]
3.201
PHE243[B]
3.641
THR245[B]
2.837
GLU246[B]
3.718
THR247[B]
3.563
ASN283[B]
4.731
Ligand Name: Tacrine Ligand Info
Structure Description Histamine Methyltransferase (Natural Variant I105) Complexed with the Acetylcholinesterase Inhibitor and Altzheimer's Disease Drug Tacrine PDB:2AOW
Method X-ray diffraction Resolution 2.97 Å Mutation Yes [1]
PDB Sequence
MRSLFSDHGK
14
YVESFRRFLN
24
HSTEHQCMQE
34
FMDKKLPGII
44
GRIGDTKSEI
54

KILSIGGGAG
64
EIDLQILSKV
74
QAQYPGVCIN
84
NEVVEPSAEQ
94
IAKYKELVAK
104

ISNLENVKFA
114
WHKETSSEYQ
124
SRMLEKKELQ
134
KWDFIHMIQM
144
LYYVKDIPAT
154

LKFFHSLLGT
164
NAKMLIIVVS
174
GSSGWDKLWK
184
KYGSRFPQDD
194
LCQYITSDDL
204

TQMLDNLGLK
214
YECYDLLSTM
224
DISDCFIDGN
234
ENGDLLWDFL
244
TETCNFNATA
254

PPDLRAELGK
264
DLQEPEFSAK
274
KEGKVLFNNT
284
LSFIVIEA
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .THA or .THA2 or .THA3 or :3THA;style chemicals stick;color identity;select .A:15 or .A:19 or .A:22 or .A:28 or .A:143 or .A:146 or .A:147 or .A:173 or .A:179 or .A:183 or .A:243 or .A:246 or .A:283; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
TYR15
4.387
PHE19
3.744
PHE22
3.424
GLU28
2.985
GLN143
3.317
TYR146
4.299
TYR147
3.372
Residue
Distance (Å)
VAL173
4.217
TRP179
3.588
TRP183
3.218
PHE243
4.325
GLU246
3.325
ASN283
4.029
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: Metoprine Ligand Info
Structure Description Histamine Methyltransferase Complexed with the Antifolate Drug Metoprine PDB:2AOV
Method X-ray diffraction Resolution 2.48 Å Mutation No [1]
PDB Sequence
MRSLFSDHGK
14
YVESFRRFLN
24
HSTEHQCMQE
34
FMDKKLPGII
44
GRIGDTKSEI
54

KILSIGGGAG
64
EIDLQILSKV
74
QAQYPGVCIN
84
NEVVEPSAEQ
94
IAKYKELVAK
104

TSNLENVKFA
114
WHKETSSEYQ
124
SRMLEKKELQ
134
KWDFIHMIQM
144
LYYVKDIPAT
154

LKFFHSLLGT
164
NAKMLIIVVS
174
GSSGWDKLWK
184
KYGSRFPQDD
194
LCQYITSDDL
204

TQMLDNLGLK
214
YECYDLLSTM
224
DISDCFIDGN
234
ENGDLLWDFL
244
TETCNFNATA
254

PPDLRAELGK
264
DLQEPEFSAK
274
KEGKVLFNNT
284
LSFIVIEA
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .C2M or .C2M2 or .C2M3 or :3C2M;style chemicals stick;color identity;select .A:15 or .A:19 or .A:22 or .A:28 or .A:143 or .A:146 or .A:147 or .A:173 or .A:179 or .A:183 or .A:196 or .A:197 or .A:198 or .A:199 or .A:243 or .A:244 or .A:246 or .A:283; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
TYR15
3.571
PHE19
4.077
PHE22
3.974
GLU28
2.535
GLN143
3.414
TYR146
3.591
TYR147
2.787
VAL173
3.562
TRP179
3.434
Residue
Distance (Å)
TRP183
3.657
CYS196
4.589
GLN197
3.016
TYR198
3.373
ILE199
4.848
PHE243
4.028
LEU244
4.789
GLU246
3.989
ASN283
4.861
Ligand Name: Cysteine Sulfenic Acid Ligand Info
Structure Description Histamine Methyltransferase Complexed with the Antihistamine Drug Diphenhydramine PDB:2AOT
Method X-ray diffraction Resolution 1.90 Å Mutation Yes [1]
PDB Sequence
> Chain A
MRSLFSDHGK
14
YVESFRRFLN
24
HSTEHQCMQE
34
FMDKKLPGII
44
GRIGDTKSEI
54

KILSIGGGAG
64
EIDLQILSKV
74
QAQYPGVCIN
84
NEVVEPSAEQ
94
IAKYKELVAK
104

TSNLENVKFA
114
WHKETSSEYQ
124
SRMLEKKELQ
134
KWDFIHMIQM
144
LYYVKDIPAT
154

LKFFHSLLGT
164
NAKMLIIVVS
174
GSSGWDKLWK
184
KYGSRFPQDD
194
LCQYITSDDL
204

TQMLDNLGLK
214
YEYDLLSTMD
225
ISDCFIDGNE
235
NGDLLWDFLT
245
ETNFNATAPP
256

DLRAELGKDL
266
QEPEFSAKKE
276
GKVLFNNTLS
286
FIVIEA
> Chain B
MRSLFSDHGK
14
YVESFRRFLN
24
HSTEHQCMQE
34
FMDKKLPGII
44
GRIGDTKSEI
54

KILSIGGGAG
64
EIDLQILSKV
74
QAQYPGVINN
85
EVVEPSAEQI
95
AKYKELVAKT
105

SNLENVKFAW
115
HKETSSEYQS
125
RMLEKKELQK
135
WDFIHMIQML
145
YYVKDIPATL
155

KFFHSLLGTN
165
AKMLIIVVSG
175
SSGWDKLWKK
185
YGSRFPQDDL
195
CQYITSDDLT
205

QMLDNLGLKY
215
ECYDLLSTMD
225
ISDCFIDGNE
235
NGDLLWDFLT
245
ETNFNATAPP
256

DLRAELGKDL
266
QEPEFSAKKE
276
GKVLFNNTLS
286
FIVIEA
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CSO or .CSO2 or .CSO3 or :3CSO;style chemicals stick;color identity;select .A:6 or .A:7 or .A:8 or .A:10 or .A:11 or .A:14 or .A:201 or .A:205 or .A:215 or .A:216 or .A:218 or .A:219 or .A:242 or .A:246 or .A:247 or .A:249 or .A:250 or .A:253 or .A:286 or .A:287 or .A:288 or .B:113 or .B:6 or .B:7 or .B:8 or .B:10 or .B:11 or .B:14 or .B:52 or .B:53 or .B:54 or .B:80 or .B:81 or .B:83 or .B:84 or .B:109 or .B:110 or .B:242 or .B:246 or .B:247 or .B:249 or .B:250 or .B:253; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ARG6[A]
2.863
SER7[A]
3.733
LEU8[A]
3.679
SER10[A]
4.108
ASP11[A]
3.139
LYS14[A]
3.316
SER201[A]
3.100
THR205[A]
3.493
TYR215[A]
4.353
GLU216[A]
1.330
TYR218[A]
1.328
ASP219[A]
3.891
ASP242[A]
3.485
GLU246[A]
4.520
THR247[A]
1.328
ASN249[A]
1.331
PHE250[A]
3.548
THR253[A]
4.188
SER286[A]
3.793
PHE287[A]
3.373
ILE288[A]
3.617
PHE113[B]
4.817
Residue
Distance (Å)
ARG6[B]
2.980
SER7[B]
3.549
LEU8[B]
3.664
SER10[B]
4.376
ASP11[B]
2.945
LYS14[B]
4.586
SER52[B]
4.134
GLU53[B]
3.449
ILE54[B]
2.900
GLY80[B]
3.635
VAL81[B]
1.331
ILE83[B]
1.321
ASN84[B]
4.305
GLU109[B]
4.976
ASN110[B]
3.543
ASP242[B]
4.101
GLU246[B]
4.489
THR247[B]
1.330
ASN249[B]
1.327
PHE250[B]
3.252
THR253[B]
3.871
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: Mepacrine Ligand Info
Structure Description Crystal Structure Analysis of Human Histamine Methyltransferase (Ile105 Polymorphic Variant) Complexed with AdoHcy and Antimalarial Drug Quinacrine PDB:1JQE
Method X-ray diffraction Resolution 1.91 Å Mutation Yes [2]
PDB Sequence
GKYVESFRRF
22
LNHSTEHQCM
32
QEFMDKKLPG
42
IIGRIGDTKS
52
EIKILSIGGG
62

AGEIDLQILS
72
KVQAQYPGVC
82
INNEVVEPSA
92
EQIAKYKELV
102
AKISNLENVK
112

FAWHKETSSE
122
YQSRMLEKKE
132
LQKWDFIHMI
142
QMLYYVKDIP
152
ATLKFFHSLL
162

GTNAKMLIIV
172
VSGSSGWDKL
182
WKKYGSRFPQ
192
DDLCQYITSD
202
DLTQMLDNLG
212

LKYECYDLLS
222
TMDISDCFID
232
GNENGDLLWD
242
FLTETCNFNA
252
TAPPDLRAEL
262

GKDLQEPEFS
272
AKKEGKVLFN
282
NTLSFIVIEA
292
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .QUN or .QUN2 or .QUN3 or :3QUN;style chemicals stick;color identity;select .A:15 or .A:16 or .A:18 or .A:19 or .A:94 or .A:146 or .A:147 or .A:173 or .A:179 or .A:183 or .A:193 or .A:195 or .A:196 or .A:197 or .A:198 or .A:243 or .A:246; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
TYR15
3.336
VAL16
3.468
SER18
4.395
PHE19
3.962
GLN94
4.233
TYR146
3.376
TYR147
3.213
VAL173
3.981
TRP179
3.667
Residue
Distance (Å)
TRP183
3.549
ASP193
3.207
LEU195
3.605
CYS196
3.645
GLN197
3.979
TYR198
4.313
PHE243
3.179
GLU246
3.487
Ligand Name: D-cysteine Ligand Info
Structure Description Histamine Methyltransferase Complexed with the Antimalarial Drug Amodiaquine PDB:2AOU
Method X-ray diffraction Resolution 2.30 Å Mutation Yes [1]
PDB Sequence
MRSLFSDHGK
14
YVESFRRFLN
24
HSTEHQCMQE
34
FMDKKLPGII
44
GRIGDTKSEI
54

KILSIGGGAG
64
EIDLQILSKV
74
QAQYPGVCIN
84
NEVVEPSAEQ
94
IAKYKELVAK
104

TSNLENVKFA
114
WHKETSSEYQ
124
SRMLEKKELQ
134
KWDFIHMIQM
144
LYYVKDIPAT
154

LKFFHSLLGT
164
NAKMLIIVVS
174
GSSGWDKLWK
184
KYGSRFPQDD
194
LCQYITSDDL
204

TQMLDNLGLK
214
YEYDLLSTMD
225
ISDCFIDGNE
235
NGDLLWDFLT
245
ETNFNATAPP
256

DLRAELGKDL
266
QEPEFSAKKE
276
GKVLFNNTLS
286
FIVIEA
Click to Show 3D Structure of This Binding Site
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Residue
Distance (Å)
MET5
4.812
ARG6
2.622
SER7
2.758
LEU8
3.534
SER10
4.044
ASP11
4.043
LYS14
3.012
Residue
Distance (Å)
ASP242
4.134
GLU246
4.468
THR247
1.330
ASN249
1.332
PHE250
3.258
THR253
4.030
Ligand Name: 4-(DIMETHYLAMINO)BUTYL IMIDOTHIOCARBAMATE Ligand Info
Structure Description Histamine Methyltransferase Complexed with the Antifolate Drug Metoprine PDB:2AOV
Method X-ray diffraction Resolution 2.48 Å Mutation No [1]
PDB Sequence
MRSLFSDHGK
14
YVESFRRFLN
24
HSTEHQCMQE
34
FMDKKLPGII
44
GRIGDTKSEI
54

KILSIGGGAG
64
EIDLQILSKV
74
QAQYPGVCIN
84
NEVVEPSAEQ
94
IAKYKELVAK
104

TSNLENVKFA
114
WHKETSSEYQ
124
SRMLEKKELQ
134
KWDFIHMIQM
144
LYYVKDIPAT
154

LKFFHSLLGT
164
NAKMLIIVVS
174
GSSGWDKLWK
184
KYGSRFPQDD
194
LCQYITSDDL
204

TQMLDNLGLK
214
YECYDLLSTM
224
DISDCFIDGN
234
ENGDLLWDFL
244
TETCNFNATA
254

PPDLRAELGK
264
DLQEPEFSAK
274
KEGKVLFNNT
284
LSFIVIEA
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Residue
Distance (Å)
TYR15
3.524
PHE19
4.683
ILE59
4.280
GLY60
3.991
VAL88
4.290
GLU89
3.986
PRO90
3.831
Residue
Distance (Å)
GLU118
4.891
THR119
3.949
SER120
3.848
MET144
3.573
TYR147
3.954
VAL148
4.943
References  Top
REF 1 Structural basis for inhibition of histamine N-methyltransferase by diverse drugs. J Mol Biol. 2005 Oct 21;353(2):334-344.
REF 2 Two polymorphic forms of human histamine methyltransferase: structural, thermal, and kinetic comparisons. Structure. 2001 Sep;9(9):837-49.

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