3FIX

Crystal structure of a putative n-acetyltransferase (ta0374) from thermoplasma acidophilum

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004145	molecular_function	diamine N-acetyltransferase activity
A	0016746	molecular_function	acyltransferase activity
A	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
A	0043939	biological_process	negative regulation of sporulation
B	0004145	molecular_function	diamine N-acetyltransferase activity
B	0016746	molecular_function	acyltransferase activity
B	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
B	0043939	biological_process	negative regulation of sporulation
C	0004145	molecular_function	diamine N-acetyltransferase activity
C	0016746	molecular_function	acyltransferase activity
C	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
C	0043939	biological_process	negative regulation of sporulation
D	0004145	molecular_function	diamine N-acetyltransferase activity
D	0016746	molecular_function	acyltransferase activity
D	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
D	0043939	biological_process	negative regulation of sporulation

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO A 160

Chain	Residue
A	THR99

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P0A951

Chain	Residue	Details
A	TYR138
B	TYR138
C	TYR138
D	TYR138

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site_id	SWS_FT_FI2
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269|PubMed:21633970

Chain	Residue	Details
A	LEU92
B	LYS140
C	LEU92
C	THR99
C	ASN131
C	SER136
C	LYS140
D	LEU92
D	THR99
D	ASN131
D	SER136
A	THR99
D	LYS140
A	ASN131
A	SER136
A	LYS140
B	LEU92
B	THR99
B	ASN131
B	SER136

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site_id	SWS_FT_FI3
Number of Residues	4
Details	SITE: May have an important role in the acetylation of the polyamine => ECO:0000250|UniProtKB:P21340

Chain	Residue	Details
A	GLY142
B	GLY142
C	GLY142
D	GLY142

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