7VNO

Structure of aminotransferase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008483	molecular_function	transaminase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0042802	molecular_function	identical protein binding
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. LIdDEVqm.GMgRtGrmwaiehfdivp....DIVtvAKalgGG

Chain	Residue	Details
A	LEU261-GLY298

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:35337912, ECO:0007744|PDB:7VNO, ECO:0007744|PDB:7VNT

Chain	Residue	Details
A	GLY124
A	THR125
A	GLN267
A	THR321
B	GLY124
B	THR125
B	GLN267
B	THR321

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site_id	SWS_FT_FI2
Number of Residues	2
Details	SITE: Plays critical role in maintaining high affinity for the substrate => ECO:0000305|PubMed:35337912

Chain	Residue	Details
A	ASP93
B	ASP93

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:35337912, ECO:0007744|PDB:7VNT

Chain	Residue	Details
A	LYS293
B	LYS293

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