4B5O

Crystal structure of human alpha tubulin acetyltransferase catalytic domain

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	7
Details	BINDING SITE FOR RESIDUE NA A 1196

Chain	Residue
A	ALA57
A	GLU128
A	GLN131
A	LYS162
A	LYS162
A	ACO1197
A	HOH2177

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site_id	AC2
Number of Residues	36
Details	BINDING SITE FOR RESIDUE ACO A 1197

Chain	Residue
A	ILE121
A	ASP123
A	PHE124
A	TYR125
A	ILE126
A	GLN131
A	ARG132
A	HIS133
A	GLY134
A	GLY136
A	ARG137
A	ASP157
A	ARG158
A	SER160
A	LYS162
A	LYS165
A	PHE166
A	LYS169
A	HIS170
A	NA1196
A	HOH2167
A	HOH2181
A	HOH2276
A	HOH2277
A	HOH2279
A	HOH2280
A	HOH2281
A	HOH2395
A	HOH2396
A	HOH2397
A	HOH2398
A	HOH2399
A	HOH2400
A	HOH2401
A	LYS56
A	GLN58

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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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