1W7L

Crystal structure of human kynurenine aminotransferase I

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0008483	molecular_function	transaminase activity
A	0009058	biological_process	biosynthetic process
A	0009617	biological_process	response to bacterium
A	0016212	molecular_function	kynurenine-oxoglutarate transaminase activity
A	0016740	molecular_function	transferase activity
A	0016829	molecular_function	lyase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0042803	molecular_function	protein homodimerization activity
A	0047316	molecular_function	glutamine-phenylpyruvate transaminase activity
A	0047804	molecular_function	cysteine-S-conjugate beta-lyase activity
A	0070189	biological_process	kynurenine metabolic process
A	0097053	biological_process	L-kynurenine catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP A 1247

Chain	Residue
A	TYR63
A	TYR216
A	SER244
A	LYS247
A	LYS255
A	HOH2108
A	HOH2324
A	HOH2327
A	GLY99
A	GLY100
A	TYR101
A	PHE125
A	ASN181
A	ASN185
A	ASP213
A	VAL215

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:15364907, ECO:0007744|PDB:1W7M

Chain	Residue	Details
A	GLY36
A	ASN185
A	ARG398

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:15364907, ECO:0007744|PDB:1W7L, ECO:0007744|PDB:1W7M

Chain	Residue	Details
A	LYS247

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