8HT4

Crystal structure of Acetylornithine aminotransferase complex with PLP from Corynebacterium glutamicum

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003992	molecular_function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
A	0005737	cellular_component	cytoplasm
A	0006525	biological_process	arginine metabolic process
A	0006526	biological_process	arginine biosynthetic process
A	0008483	molecular_function	transaminase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0042802	molecular_function	identical protein binding
B	0003992	molecular_function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
B	0005737	cellular_component	cytoplasm
B	0006525	biological_process	arginine metabolic process
B	0006526	biological_process	arginine biosynthetic process
B	0008483	molecular_function	transaminase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0042802	molecular_function	identical protein binding

Functional Information from PROSITE/UniProt

site_id	PS00600
Number of Residues	38
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. MItDEVqt.GVgRtGdffahqhdgvvp....DVVtmAKglgGG

Chain	Residue	Details
A	MET221-GLY258

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01107

Chain	Residue	Details
A	GLY110
B	ASP224
B	THR281
B	THR282
A	PHE136
A	ARG139
A	ASP224
A	THR281
A	THR282
B	GLY110
B	PHE136
B	ARG139

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site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_01107

Chain	Residue	Details
A	LYS253
B	LYS253

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