4U9Y

Structure of the alpha-tubulin acetyltransferase alpha-TAT1/Mec-17 in complex with CoA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005874	cellular_component	microtubule
A	0019799	molecular_function	tubulin N-acetyltransferase activity
A	0071929	biological_process	alpha-tubulin acetylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	31
Details	binding site for residue COA A 201

Chain	Residue
A	LYS56
A	GLY134
A	HIS135
A	GLY136
A	ARG137
A	ARG158
A	SER160
A	LYS162
A	LYS165
A	PHE166
A	LYS169
A	GLN58
A	HIS170
A	HOH308
A	HOH310
A	HOH315
A	HOH325
A	HOH350
A	HOH366
A	HOH388
A	HOH391
A	HOH393
A	PHE124
A	HOH395
A	HOH406
A	TYR125
A	ILE126
A	GLU128
A	GLN131
A	ARG132
A	HIS133

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site_id	AC2
Number of Residues	5
Details	binding site for residue BR A 202

Chain	Residue
A	SER66
A	ARG69
A	MET70
A	HIS75
A	LYS98

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:23071314, ECO:0000269|PubMed:23071318, ECO:0000269|PubMed:24906155

Chain	Residue	Details
A	PHE124
A	SER160

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site_id	SWS_FT_FI2
Number of Residues	1
Details	SITE: Crucial for catalytic activity => ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:23071318

Chain	Residue	Details
A	GLN58

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000250|UniProtKB:Q8K341, ECO:0000255|HAMAP-Rule:MF_03130

Chain	Residue	Details
A	LYS56
A	LYS146

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