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 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
Ligand General Information  Top
Ligand Name Acetyl CoA Ligand Info
Canonical SMILES CC(=O)SCCNC(=O)CCNC(=O)C(C(C)(C)COP(=O)(O)OP(=O)(O)OCC1C(C(C(O1)N2C=NC3=C(N=CN=C32)N)O)OP(=O)(O)O)O
InChI 1S/C23H38N7O17P3S/c1-12(31)51-7-6-25-14(32)4-5-26-21(35)18(34)23(2,3)9-44-50(41,42)47-49(39,40)43-8-13-17(46-48(36,37)38)16(33)22(45-13)30-11-29-15-19(24)27-10-28-20(15)30/h10-11,13,16-18,22,33-34H,4-9H2,1-3H3,(H,25,32)(H,26,35)(H,39,40)(H,41,42)(H2,24,27,28)(H2,36,37,38)/t13-,16-,17-,18+,22-/m1/s1
InChIKey ZSLZBFCDCINBPY-ZSJPKINUSA-N
PubChem Compound ID 444493
Drug Binding Sites of Target  Top
PDB ID: 4GS4      Structure of the alpha-tubulin acetyltransferase, alpha-TAT1
Method X-ray diffraction Resolution 2.11 Å Mutation No [1]
PDB Sequence
FPFDVDALFP
12
ERITVLDQHL
22
RPPVDLQQQI
43
TIIDELGKAS
54
AKAQNLSAPI
64

TSASRQSNRH
75
VVYILKDSAI
93
IGFIKVGYKK
103
LFVLDDREAH
113
NEVEPLCILD
123

FYIHESVQRH
133
GHGRELFQYL
144
QKERVEPHQL
154
AIDRPSQKLL
164
KFLNKHYNLE
174

TTVPQVNNFV
184
IFEGFFAHQH
194
R
Residue
Distance (Å)
ALA57
4.206
GLN58
3.326
ILE121
3.749
LEU122
3.738
ASP123
3.253
PHE124
2.837
TYR125
3.508
ILE126
2.710
VAL130
4.804
GLN131
3.569
ARG132
2.723
HIS133
3.230
GLY134
2.877
HIS135
3.714
Residue
Distance (Å)
GLY136
2.649
ARG137
2.961
ILE156
3.415
ASP157
3.520
ARG158
3.589
PRO159
3.933
SER160
2.631
LYS162
3.083
LEU163
3.400
LYS165
3.278
PHE166
3.342
LYS169
2.562
HIS170
3.135
PDB ID: 3VWD      Crystal structure of alpha-tubulin acetyltransferase domain of human Mec-17 in complex with acetoacetyl-CoA (P21212 form)
Method X-ray diffraction Resolution 1.25 Å Mutation No [2]
PDB Sequence
SMEFPFDVDA
9
LFPERITVLD
19
QHLRPPARRP
29
GTTTPARVDL
39
QQQIMTIIDE
49

LGKASAKAQN
59
LSAPITSASR
69
MQSNRHVVYI
79
LKDSSARPAG
89
AIIGFIKVGY
101

KKLFVLDDRE
111
AHNEVEPLCI
121
LDFYIHESVQ
131
RHGHGRELFQ
141
YMLQKERVEP
151

HQLAIDRPSQ
161
KLLKFLNKHY
171
NLETTVPQVN
181
NFVIFEGFFA
191
HQHEFG
Residue
Distance (Å)
ALA57
4.149
GLN58
3.222
ILE121
3.547
LEU122
3.951
ASP123
3.328
PHE124
2.732
TYR125
3.365
ILE126
2.858
VAL130
4.689
GLN131
3.540
ARG132
2.832
HIS133
3.208
GLY134
2.792
HIS135
3.787
Residue
Distance (Å)
GLY136
2.857
ARG137
2.911
ILE156
3.910
ASP157
3.138
ARG158
3.642
PRO159
3.878
SER160
2.728
LYS162
3.461
LEU163
3.767
LYS165
3.213
PHE166
3.276
LYS169
2.674
HIS170
2.996
PDB ID: 4B5O      Crystal structure of human alpha tubulin acetyltransferase catalytic domain
Method X-ray diffraction Resolution 1.05 Å Mutation No [3]
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
PDB ID: 4B5P      Crystal structure of human alpha tubulin acetyltransferase catalytic domain Q58A variant
Method X-ray diffraction Resolution 1.60 Å Mutation Yes [3]
PDB Sequence
> Chain A
ASMEFPFDVD
8
ALFPERITVL
18
DQHLRPPAPA
35
RVDLQQQIMT
45
IIDELGKASA
55

KAANLSAPIT
65
SASRMQSNRH
75
VVYILKDSSA
85
RPGKGAIIGF
96
IKVGYKKLFV
106

LDDREAHNEV
116
EPLCILDFYI
126
HESVQRHGHG
136
RELFQYMLQK
146
ERVEPHQLAI
156

DRPSQKLLKF
166
LNKHYNLETT
176
VPQVNNFVIF
186
EGFF
> Chain B
ASMEFPFDVD
8
ALFPERITVL
18
DQHLRPPAAR
36
VDLQQQIMTI
46
IDELGKASAK
56

AANLSAPITS
66
ASRMQSNRHV
76
VYILKDSSAA
92
IIGFIKVGYK
102
KLFVLDDREA
112

HNEVEPLCIL
122
DFYIHESVQR
132
HGHGRELFQY
142
MLQKERVEPH
152
QLAIDRPSQK
162

LLKFLNKHYN
172
LETTVPQVNN
182
FVIFEGFFAH
192
QHRP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ACO or .ACO2 or .ACO3 or :3ACO;style chemicals stick;color identity;select .A:54 or .A:57 or .A:58 or .A:121 or .A:122 or .A:123 or .A:124 or .A:125 or .A:126 or .A:128 or .A:130 or .A:131 or .A:132 or .A:133 or .A:134 or .A:135 or .A:136 or .A:137 or .A:138 or .A:156 or .A:157 or .A:158 or .A:159 or .A:160 or .A:162 or .A:163 or .A:165 or .A:166 or .A:169 or .A:170 or .A:53 or .A:56 or .A:59 or .A:125 or .A:128 or .B:53 or .B:56 or .B:57 or .B:59 or .B:125 or .B:128 or .B:54 or .B:57 or .B:58 or .B:64 or .B:121 or .B:122 or .B:123 or .B:124 or .B:125 or .B:126 or .B:128 or .B:130 or .B:131 or .B:132 or .B:133 or .B:134 or .B:135 or .B:136 or .B:137 or .B:138 or .B:156 or .B:157 or .B:158 or .B:159 or .B:160 or .B:162 or .B:163 or .B:165 or .B:166 or .B:169 or .B:170; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue [Chain]
Distance (Å)
SER54[A]
4.142
ALA57[A]
2.448
ALA58[A]
3.392
ILE121[A]
2.433
LEU122[A]
3.442
ASP123[A]
2.691
PHE124[A]
1.895
TYR125[A]
2.554
ILE126[A]
2.056
GLU128[A]
4.813
VAL130[A]
4.646
GLN131[A]
2.476
ARG132[A]
1.998
HIS133[A]
3.046
GLY134[A]
2.018
HIS135[A]
3.491
GLY136[A]
2.087
ARG137[A]
2.019
GLU138[A]
4.545
ILE156[A]
2.578
ASP157[A]
2.294
ARG158[A]
3.752
PRO159[A]
3.038
SER160[A]
1.904
LYS162[A]
2.280
LEU163[A]
2.486
LYS165[A]
2.829
PHE166[A]
2.645
LYS169[A]
2.195
HIS170[A]
2.096
ALA53[A]
4.518
LYS56[A]
3.057
ASN59[A]
4.313
TYR125[A]
4.686
GLU128[A]
3.447
ALA53[B]
4.609
Residue [Chain]
Distance (Å)
LYS56[B]
2.723
ALA57[B]
4.979
ASN59[B]
4.502
TYR125[B]
4.588
GLU128[B]
3.496
SER54[B]
4.027
ALA57[B]
2.466
ALA58[B]
3.414
ILE64[B]
4.990
ILE121[B]
2.456
LEU122[B]
3.320
ASP123[B]
2.568
PHE124[B]
1.880
TYR125[B]
2.480
ILE126[B]
2.064
GLU128[B]
4.940
VAL130[B]
4.597
GLN131[B]
2.472
ARG132[B]
1.932
HIS133[B]
3.125
GLY134[B]
2.028
HIS135[B]
3.529
GLY136[B]
2.214
ARG137[B]
2.085
GLU138[B]
4.461
ILE156[B]
2.490
ASP157[B]
2.286
ARG158[B]
3.602
PRO159[B]
3.078
SER160[B]
1.951
LYS162[B]
2.308
LEU163[B]
2.466
LYS165[B]
2.779
PHE166[B]
2.587
LYS169[B]
1.778
HIS170[B]
2.153
PDB ID: 4IF5      Structure of human Mec17
Method X-ray diffraction Resolution 1.70 Å Mutation No [4]
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 .ACO or .ACO2 or .ACO3 or :3ACO;style chemicals stick;color identity;select .A:57 or .A:58 or .A:121 or .A:122 or .A:123 or .A:124 or .A:125 or .A:126 or .A:130 or .A:131 or .A:132 or .A:133 or .A:134 or .A:135 or .A:136 or .A:137 or .A:156 or .A:157 or .A:158 or .A:159 or .A:160 or .A:162 or .A:163 or .A:165 or .A:166 or .A:169 or .A:170; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ALA57
4.139
GLN58
3.348
ILE121
3.526
LEU122
4.077
ASP123
3.368
PHE124
2.671
TYR125
3.392
ILE126
2.842
VAL130
4.586
GLN131
3.461
ARG132
2.788
HIS133
3.279
GLY134
2.772
HIS135
3.803
Residue
Distance (Å)
GLY136
2.886
ARG137
2.887
ILE156
3.691
ASP157
3.075
ARG158
3.693
PRO159
3.880
SER160
2.720
LYS162
3.399
LEU163
3.759
LYS165
3.183
PHE166
3.333
LYS169
2.607
HIS170
2.910
References  Top
REF 1 Structure of the Alpha-tubulin acetyltransferase, AlphaTAT1, and implications for tubulin-specific acetylation. Proc Natl Acad Sci U S A. 2012 Nov 27;109(48):19655-60.
REF 2 Crystal structure of alpha-tubulin acetyltransferase domain of human Mec-17
REF 3 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 4 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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