Structure of PDB 4h6u Chain A Binding Site BS01

Receptor Information
>4h6u Chain A (length=165) Species: 7955 (Danio rerio) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SFTMDFPYDLNALFPERISVLDSNLSAGRKAHGRPDPLPQVTTVIDELGK
NRHHLYLLKDGEGGRGVIVGFLKVGYKKLFLLDQRGAHLETEPLCVLAFY
VTETLQRHGYGSELFDFMLKHKQVEPAQMAYDRPSPKFLSFLEKRYDLRN
SVPQVNNFVVFAGFF
Ligand information
Ligand IDACO
InChIInChI=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
InChIKeyZSLZBFCDCINBPY-ZSJPKINUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)O
CACTVS 3.341CC(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)CO[P@@](O)(=O)O[P@](O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O[P](O)(O)=O)n2cnc3c(N)ncnc23
ACDLabs 10.04O=C(SCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3OP(=O)(O)O)C
CACTVS 3.341CC(=O)SCCNC(=O)CCNC(=O)[CH](O)C(C)(C)CO[P](O)(=O)O[P](O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O[P](O)(O)=O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0CC(=O)SCCNC(=O)CCNC(=O)C(C(C)(C)COP(=O)(O)OP(=O)(O)OCC1C(C(C(O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)O
FormulaC23 H38 N7 O17 P3 S
NameACETYL COENZYME *A
ChEMBLCHEMBL1230809
DrugBank
ZINCZINC000008551095
PDB chain4h6u Chain A Residue 201 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB4h6u Crystal structures of tubulin acetyltransferase reveal a conserved catalytic core and the plasticity of the essential N terminus.
Resolution2.4482 Å
Binding residue
(original residue number in PDB)		A117 F118 Y119 V120 Q125 R126 G128 G130 S131 P153 S154 K156 F157 S159 F160 K163 R164
Binding residue
(residue number reindexed from 1)		A98 F99 Y100 V101 Q106 R107 G109 G111 S112 P134 S135 K137 F138 S140 F141 K144 R145
Annotation score4
Enzymatic activity
Enzyme Commision number 2.3.1.108: alpha-tubulin N-acetyltransferase.
Gene Ontology
Molecular Function
GO:0019799 tubulin N-acetyltransferase activity
Biological Process
GO:0071929 alpha-tubulin acetylation
Cellular Component
GO:0005874 microtubule

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4h6u, PDBe:4h6u, PDBj:4h6u
PDBsum4h6u
PubMed23105108
UniProtQ6PH17|ATAT_DANRE Alpha-tubulin N-acetyltransferase 1 (Gene Name=atat1)

[Back to BioLiP]