Binding Site Information of Target

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Target General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T92639 Target Info
Target Name Alpha-tubulin N-acetyltransferase 1 (ATAT1)
Synonyms MEC17; C6orf134; Alpha-TAT; Acetyltransferase mec-17 homolog
Target Type Literature-reported Target
Gene Name ATAT1
Biochemical Class Acetyltransferase ATAT1 family
UniProt ID
ATAT_HUMAN
Drug Binding Sites of Target  Top
Ligand Name: Acetyl CoA Ligand Info
Structure Description Crystal structure of human alpha tubulin acetyltransferase catalytic domain PDB:4B5O
Method X-ray diffraction Resolution 1.05 Å Mutation No [1]
PDB Sequence
SMEFPFDVDA
9
LFPERITVLD
19
QHLRPPARRP
29
GTTTPARVDL
39
QQQIMTIIDE
49

LGKASAKAQN
59
LSAPITSASR
69
MQSNRHVVYI
79
LKDSSARPAI
93
IGFIKVGYKK
103

LFVLDDREAH
113
NEVEPLCILD
123
FYIHESVQRH
133
GHGRELFQYM
143
LQKERVEPHQ
153

LAIDRPSQKL
163
LKFLNKHYNL
173
ETTVPQVNNF
183
VIFEGFFAHQ
193
HR
Residue
Distance (Å)
SER54
4.612
ALA57
2.854
GLN58
2.821
ILE64
4.836
ILE121
2.664
LEU122
3.204
ASP123
2.606
PHE124
1.903
TYR125
2.491
ILE126
2.089
GLU128
4.782
VAL130
4.674
GLN131
2.384
ARG132
1.948
HIS133
3.006
GLY134
2.011
Residue
Distance (Å)
HIS135
3.486
GLY136
2.057
ARG137
2.111
GLU138
4.722
ILE156
2.495
ASP157
2.297
ARG158
3.629
PRO159
2.973
SER160
1.956
LYS162
2.376
LEU163
2.458
LYS165
2.774
PHE166
2.577
LYS169
1.850
HIS170
2.195
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: Coenzyme A Ligand Info
Structure Description tubulin acetyltransferase complex with bisubstrate analog PDB:4PK2
Method X-ray diffraction Resolution 1.35 Å Mutation No [2]
PDB Sequence
FTMEFPFDVD
8
ALFPERITVL
18
DQHLRPPAVD
38
LQQQIMTIID
48
ELGKASAKAQ
58

NLSAPITSAS
68
RMQSNRHVVY
78
ILKDSSARPA
88
GKGAIIGFIK
98
VGYKKLFVLD
108

DREAHNEVEP
118
LCILDFYIHE
128
SVQRHGHGRE
138
LFQYMLQKER
148
VEPHQLAIDR
158

PSQKLLKFLN
168
KHYNLETTVP
178
QVNNFVIFEG
188
FFAHQHPP
Residue
Distance (Å)
SER54
4.798
ALA57
3.404
GLN58
3.449
ASP123
4.794
PHE124
2.810
TYR125
2.515
ILE126
2.125
VAL130
4.647
GLN131
3.000
ARG132
1.916
HIS133
3.239
GLY134
2.062
HIS135
3.378
GLY136
2.060
Residue
Distance (Å)
ARG137
2.196
GLU138
4.694
ILE156
4.395
ASP157
4.598
ARG158
4.220
PRO159
2.791
SER160
2.090
LYS162
2.729
LEU163
3.113
LYS165
3.149
PHE166
2.708
LYS169
1.744
HIS170
2.227
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: (2S)-2-amino-6-(propanoylamino)hexanoic acid Ligand Info
Structure Description tubulin acetyltransferase complex with bisubstrate analog PDB:4PK2
Method X-ray diffraction Resolution 1.35 Å Mutation No [2]
PDB Sequence
FTMEFPFDVD
8
ALFPERITVL
18
DQHLRPPAVD
38
LQQQIMTIID
48
ELGKASAKAQ
58

NLSAPITSAS
68
RMQSNRHVVY
78
ILKDSSARPA
88
GKGAIIGFIK
98
VGYKKLFVLD
108

DREAHNEVEP
118
LCILDFYIHE
128
SVQRHGHGRE
138
LFQYMLQKER
148
VEPHQLAIDR
158

PSQKLLKFLN
168
KHYNLETTVP
178
QVNNFVIFEG
188
FFAHQHPP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .PRK or .PRK2 or .PRK3 or :3PRK;style chemicals stick;color identity;select .A:54 or .A:58 or .A:60 or .A:64 or .A:121 or .A:122 or .A:123 or .A:124 or .A:156 or .A:157 or .A:158 or .A:159 or .A:160 or .A:163 or .A:182; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER54
4.955
GLN58
2.125
LEU60
3.867
ILE64
2.987
ILE121
2.960
LEU122
3.489
ASP123
2.321
PHE124
3.373
Residue
Distance (Å)
ILE156
3.551
ASP157
2.842
ARG158
2.890
PRO159
3.249
SER160
4.056
LEU163
3.390
ASN182
3.785
Ligand Name: N6-Acetyl-L-lysine Ligand Info
Structure Description tubulin acetyltransferase complex with bisubstrate analog PDB:4PK3
Method X-ray diffraction Resolution 1.35 Å Mutation No [2]
PDB Sequence
FTMEFPFDVD
8
ALFPERITVL
18
DQHLRPPAVD
38
LQQQIMTIID
48
ELGKASAKAQ
58

NLSAPITSAS
68
RMQSNRHVVY
78
ILKDSSARPA
88
GKGAIIGFIK
98
VGYKKLFVLD
108

DREAHNEVEP
118
LCILDFYIHE
128
SVQRHGHGRE
138
LFQYMLQKER
148
VEPHQLAIDR
158

PSQKLLKFLN
168
KHYNLETTVP
178
QVNNFVIFEG
188
FFAHQHPP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ALY or .ALY2 or .ALY3 or :3ALY;style chemicals stick;color identity;select .A:54 or .A:58 or .A:60 or .A:64 or .A:121 or .A:122 or .A:123 or .A:124 or .A:156 or .A:157 or .A:158 or .A:159 or .A:160 or .A:163 or .A:182; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER54
4.494
GLN58
2.314
LEU60
2.533
ILE64
2.342
ILE121
3.656
LEU122
2.369
ASP123
2.208
PHE124
2.912
Residue
Distance (Å)
ILE156
2.773
ASP157
2.556
ARG158
2.498
PRO159
2.967
SER160
4.169
LEU163
3.280
ASN182
2.761
Ligand Name: Selenomethionine Ligand Info
Structure Description Structure of human Mec17 PDB:4IF5
Method X-ray diffraction Resolution 1.70 Å Mutation No [3]
PDB Sequence
HEFPFDVDAL
10
FPERITVLDQ
20
HLRPPARRPG
30
TTTPARVDLQ
40
QQITIIDELG
51

KASAKAQNLS
61
APITSASRQS
72
NRHVVYILKD
82
SSARPAGKGA
92
IIGFIKVGYK
102

KLFVLDDREA
112
HNEVEPLCIL
122
DFYIHESVQR
132
HGHGRELFQY
142
LQKERVEPHQ
153

LAIDRPSQKL
163
LKFLNKHYNL
173
ETTVPQVNNF
183
VIFEGFFA
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .MSE or .MSE2 or .MSE3 or :3MSE;style chemicals stick;color identity;select .A:-1 or .A:2 or .A:3 or .A:18 or .A:19 or .A:20 or .A:22 or .A:40 or .A:41 or .A:42 or .A:43 or .A:45 or .A:46 or .A:47 or .A:48 or .A:49 or .A:50 or .A:53 or .A:66 or .A:67 or .A:68 or .A:69 or .A:71 or .A:72 or .A:73 or .A:74 or .A:75 or .A:76 or .A:77 or .A:78 or .A:91 or .A:92 or .A:93 or .A:94 or .A:95 or .A:97 or .A:98 or .A:99 or .A:119 or .A:121 or .A:125 or .A:127 or .A:139 or .A:140 or .A:141 or .A:142 or .A:144 or .A:145 or .A:146 or .A:147 or .A:148 or .A:149 or .A:154; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
HIS-1
1.331
GLU2
1.330
PHE3
3.718
LEU18
3.630
ASP19
3.669
GLN20
3.435
LEU22
3.676
GLN40
2.865
GLN41
3.244
GLN42
3.299
ILE43
1.326
THR45
1.325
ILE46
3.338
ILE47
3.471
ASP48
2.900
GLU49
4.989
LEU50
3.619
ALA53
4.396
SER66
2.870
ALA67
3.237
SER68
3.279
ARG69
1.327
GLN71
1.325
SER72
3.293
ASN73
3.077
ARG74
4.988
HIS75
3.669
Residue
Distance (Å)
VAL76
4.540
VAL77
3.775
TYR78
3.675
GLY91
4.392
ALA92
3.743
ILE93
3.267
ILE94
3.687
GLY95
4.305
ILE97
4.126
LYS98
4.224
VAL99
3.878
LEU119
4.224
ILE121
3.627
TYR125
3.889
HIS127
3.964
LEU139
3.036
PHE140
3.217
GLN141
3.306
TYR142
1.329
LEU144
1.332
GLN145
3.149
LYS146
3.248
GLU147
2.858
ARG148
4.526
VAL149
4.602
LEU154
4.640
Click to View More Binding Site Information of This Target and Ligand Pair
References  Top
REF 1 Atomic resolution structure of human Alpha-tubulin acetyltransferase bound to acetyl-CoA. Proc Natl Acad Sci U S A. 2012 Nov 27;109(48):19649-54.
REF 2 Molecular basis for age-dependent microtubule acetylation by tubulin acetyltransferase. Cell. 2014 Jun 5;157(6):1405-1415.
REF 3 Structural and functional characterization of the Alpha-tubulin acetyltransferase MEC-17. J Mol Biol. 2014 Jul 15;426(14):2605-16.

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