3VWE

Crystal structure of alpha-tubulin acetyltransferase domain of human Mec-17 in complex with CoA (P21 form)

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	19
Details	BINDING SITE FOR RESIDUE COA A 201

Chain	Residue
A	GLN58
A	ARG137
A	SER160
A	LYS162
A	LYS165
A	PHE166
A	LYS169
A	HIS170
A	HOH308
A	HOH355
A	HOH389
A	PHE124
A	TYR125
A	ILE126
A	GLN131
A	ARG132
A	HIS133
A	GLY134
A	GLY136

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	22
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03130","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23071314","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23071318","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24906155","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Site: {"description":"Crucial for catalytic activity","evidences":[{"source":"HAMAP-Rule","id":"MF_03130","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23071318","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"Q8K341","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_03130","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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