3ASA

Crystal structure of apo-LL-diaminopimelate aminotransferase from Chlamydia trachomatis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0008483	molecular_function	transaminase activity
A	0009058	biological_process	biosynthetic process
A	0009089	biological_process	lysine biosynthetic process via diaminopimelate
A	0010285	molecular_function	L,L-diaminopimelate aminotransferase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0033362	biological_process	lysine biosynthetic process via diaminopimelate, diaminopimelate-aminotransferase pathway

Functional Information from PROSITE/UniProt

site_id	PS00105
Number of Residues	14
Details	AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SFSKplGFaGIRLG

Chain	Residue	Details
A	SER233-GLY246

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q93ZN9, ECO:0000305|PubMed:21722650

Chain	Residue	Details
A	TYR14
A	TYR128
A	ASN174

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q93ZN9

Chain	Residue	Details
A	GLY41
A	TYR71
A	LYS105
A	ARG244
A	ASN275
A	ARG369

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site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:21722650

Chain	Residue	Details
A	ALA104
A	TYR205
A	SER233

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:21722650

Chain	Residue	Details
A	LYS236

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