Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4ADB

Structural and functional study of succinyl-ornithine transaminase from E. coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003992	molecular_function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
A	0006520	biological_process	amino acid metabolic process
A	0006525	biological_process	arginine metabolic process
A	0006526	biological_process	arginine biosynthetic process
A	0006527	biological_process	arginine catabolic process
A	0006593	biological_process	ornithine catabolic process
A	0008483	molecular_function	transaminase activity
A	0019544	biological_process	arginine catabolic process to glutamate
A	0019545	biological_process	arginine catabolic process to succinate
A	0030170	molecular_function	pyridoxal phosphate binding
A	0042450	biological_process	arginine biosynthetic process via ornithine
A	0042802	molecular_function	identical protein binding
A	0043825	molecular_function	succinylornithine transaminase activity
B	0003992	molecular_function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
B	0006520	biological_process	amino acid metabolic process
B	0006525	biological_process	arginine metabolic process
B	0006526	biological_process	arginine biosynthetic process
B	0006527	biological_process	arginine catabolic process
B	0006593	biological_process	ornithine catabolic process
B	0008483	molecular_function	transaminase activity
B	0019544	biological_process	arginine catabolic process to glutamate
B	0019545	biological_process	arginine catabolic process to succinate
B	0030170	molecular_function	pyridoxal phosphate binding
B	0042450	biological_process	arginine biosynthetic process via ornithine
B	0042802	molecular_function	identical protein binding
B	0043825	molecular_function	succinylornithine transaminase activity
C	0003992	molecular_function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
C	0006520	biological_process	amino acid metabolic process
C	0006525	biological_process	arginine metabolic process
C	0006526	biological_process	arginine biosynthetic process
C	0006527	biological_process	arginine catabolic process
C	0006593	biological_process	ornithine catabolic process
C	0008483	molecular_function	transaminase activity
C	0019544	biological_process	arginine catabolic process to glutamate
C	0019545	biological_process	arginine catabolic process to succinate
C	0030170	molecular_function	pyridoxal phosphate binding
C	0042450	biological_process	arginine biosynthetic process via ornithine
C	0042802	molecular_function	identical protein binding
C	0043825	molecular_function	succinylornithine transaminase activity
D	0003992	molecular_function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
D	0006520	biological_process	amino acid metabolic process
D	0006525	biological_process	arginine metabolic process
D	0006526	biological_process	arginine biosynthetic process
D	0006527	biological_process	arginine catabolic process
D	0006593	biological_process	ornithine catabolic process
D	0008483	molecular_function	transaminase activity
D	0019544	biological_process	arginine catabolic process to glutamate
D	0019545	biological_process	arginine catabolic process to succinate
D	0030170	molecular_function	pyridoxal phosphate binding
D	0042450	biological_process	arginine biosynthetic process via ornithine
D	0042802	molecular_function	identical protein binding
D	0043825	molecular_function	succinylornithine transaminase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLP A 1404

Chain	Residue
A	SER104
A	LYS252
A	HOH2128
A	HOH2166
A	HOH2168
A	HOH2217
A	HOH2218
A	HOH2219
B	THR281
A	GLY105
A	ALA106
A	PHE138
A	HIS139
A	GLU190
A	ASP223
A	VAL225
A	GLN226

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG A 1999

Chain	Residue
A	HOH2110
A	HOH2111
A	HOH2220
A	HOH2221
A	HOH2222
A	HOH2223
C	LYS118

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLP B 1404

Chain	Residue
A	THR281
A	HOH2101
A	HOH2102
A	HOH2176
A	HOH2178
B	SER104
B	GLY105
B	ALA106
B	PHE138
B	HIS139
B	GLU190
B	ASP223
B	VAL225
B	GLN226
B	LYS252
B	HOH2096
B	HOH2181

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA B 1405

Chain	Residue
B	ILE91
B	THR94
B	PHE95
B	ALA96
B	HOH2062
B	HOH2064

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MG B 1999

Chain	Residue
A	HOH2137
A	HOH2137
A	HOH2138
A	HOH2138
B	LYS118
B	LYS118
B	HOH2073
B	HOH2073

site_id	AC6
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP C 1404

Chain	Residue
C	SER104
C	GLY105
C	ALA106
C	PHE138
C	HIS139
C	GLU190
C	ASP223
C	VAL225
C	GLN226
C	LYS252
C	HOH2094
C	HOH2123
C	HOH2153
C	HOH2154
C	HOH2155
D	THR281

site_id	AC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP D 1404

Chain	Residue
C	THR281
C	HOH2073
C	HOH2130
D	SER104
D	GLY105
D	ALA106
D	PHE138
D	HIS139
D	GLU190
D	ASP223
D	VAL225
D	GLN226
D	LYS252
D	HOH2051
D	HOH2085

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA C 1405

Chain	Residue
C	ILE91
C	THR94
C	ALA96
C	HOH2063
C	HOH2065

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA A 1405

Chain	Residue
A	ILE91
A	THR94
A	ALA96
A	HOH2090
A	HOH2093

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA D 1405

Chain	Residue
D	ALA96
D	ILE91
D	THR94
D	PHE95

Functional Information from PROSITE/UniProt

site_id	PS00600
Number of Residues	38
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIfDEVqt.GVgRtGelyaymhygvtp....DLLttAKalgGG

Chain	Residue	Details
A	LEU220-GLY257

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250

Chain	Residue	Details
A	LYS252
B	LYS252
C	LYS252
D	LYS252

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)