3ASB

Crystal structure of PLP-bound 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	0016740	molecular_function	transferase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0033362	biological_process	lysine biosynthetic process via diaminopimelate, diaminopimelate-aminotransferase pathway

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE LLP A 401

Chain	Residue
A	GLY103
A	SER233
A	PHE234
A	SER235
A	PRO237
A	LEU238
A	ASN275
A	ALA104
A	LYS105
A	TYR128
A	CYS170
A	ASN174
A	ASP202
A	TYR205
A	PHE208

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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	5
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q93ZN9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21722650","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q93ZN9","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"21722650","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"21722650","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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