Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2QLR

Crystal structure of human kynurenine aminotransferase II

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0006103	biological_process	2-oxoglutarate metabolic process
A	0006536	biological_process	glutamate metabolic process
A	0008483	molecular_function	transaminase activity
A	0009058	biological_process	biosynthetic process
A	0016212	molecular_function	kynurenine-oxoglutarate transaminase activity
A	0016740	molecular_function	transferase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0033512	biological_process	L-lysine catabolic process to acetyl-CoA via saccharopine
A	0042803	molecular_function	protein homodimerization activity
A	0047315	molecular_function	kynurenine-glyoxylate transaminase activity
A	0047536	molecular_function	2-aminoadipate transaminase activity
A	0047958	molecular_function	glycine:2-oxoglutarate aminotransferase activity
A	0050094	molecular_function	methionine-glyoxylate transaminase activity
A	0070189	biological_process	kynurenine metabolic process
A	1901605	biological_process	alpha-amino acid metabolic process
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0006103	biological_process	2-oxoglutarate metabolic process
B	0006536	biological_process	glutamate metabolic process
B	0008483	molecular_function	transaminase activity
B	0009058	biological_process	biosynthetic process
B	0016212	molecular_function	kynurenine-oxoglutarate transaminase activity
B	0016740	molecular_function	transferase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0033512	biological_process	L-lysine catabolic process to acetyl-CoA via saccharopine
B	0042803	molecular_function	protein homodimerization activity
B	0047315	molecular_function	kynurenine-glyoxylate transaminase activity
B	0047536	molecular_function	2-aminoadipate transaminase activity
B	0047958	molecular_function	glycine:2-oxoglutarate aminotransferase activity
B	0050094	molecular_function	methionine-glyoxylate transaminase activity
B	0070189	biological_process	kynurenine metabolic process
B	1901605	biological_process	alpha-amino acid metabolic process
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0006103	biological_process	2-oxoglutarate metabolic process
C	0006536	biological_process	glutamate metabolic process
C	0008483	molecular_function	transaminase activity
C	0009058	biological_process	biosynthetic process
C	0016212	molecular_function	kynurenine-oxoglutarate transaminase activity
C	0016740	molecular_function	transferase activity
C	0030170	molecular_function	pyridoxal phosphate binding
C	0033512	biological_process	L-lysine catabolic process to acetyl-CoA via saccharopine
C	0042803	molecular_function	protein homodimerization activity
C	0047315	molecular_function	kynurenine-glyoxylate transaminase activity
C	0047536	molecular_function	2-aminoadipate transaminase activity
C	0047958	molecular_function	glycine:2-oxoglutarate aminotransferase activity
C	0050094	molecular_function	methionine-glyoxylate transaminase activity
C	0070189	biological_process	kynurenine metabolic process
C	1901605	biological_process	alpha-amino acid metabolic process
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
D	0006103	biological_process	2-oxoglutarate metabolic process
D	0006536	biological_process	glutamate metabolic process
D	0008483	molecular_function	transaminase activity
D	0009058	biological_process	biosynthetic process
D	0016212	molecular_function	kynurenine-oxoglutarate transaminase activity
D	0016740	molecular_function	transferase activity
D	0030170	molecular_function	pyridoxal phosphate binding
D	0033512	biological_process	L-lysine catabolic process to acetyl-CoA via saccharopine
D	0042803	molecular_function	protein homodimerization activity
D	0047315	molecular_function	kynurenine-glyoxylate transaminase activity
D	0047536	molecular_function	2-aminoadipate transaminase activity
D	0047958	molecular_function	glycine:2-oxoglutarate aminotransferase activity
D	0050094	molecular_function	methionine-glyoxylate transaminase activity
D	0070189	biological_process	kynurenine metabolic process
D	1901605	biological_process	alpha-amino acid metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL B 426

Chain	Residue
B	ASN328
B	ASP331

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL D 426

Chain	Residue
C	SER404
D	MET33
D	ILE34
D	SER35

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 427

Chain	Residue
C	HIS318
C	ARG321
C	HOH562
C	ASN57
C	TRP310
C	GLY314

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL A 426

Chain	Residue
A	THR21
A	ILE25

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL D 427

Chain	Residue
D	GLY64
D	GLU65
D	GLU66
D	MET67

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 428

Chain	Residue
C	PHE325
C	GLN329
C	SER404
C	ALA405
C	SER406
C	PRO407
D	ASN42

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL D 428

Chain	Residue
D	ASP138
D	ASP162
D	GLY165
D	VAL197
D	ASN201
D	THR204
D	ASN206
D	HOH567
D	HOH572

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 427

Chain	Residue
A	ASP162
A	GLU163
A	HIS348

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL C 429

Chain	Residue
C	SER391
D	HOH449

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL D 429

Chain	Residue
D	THR8
D	SER11
D	ARG14
D	LYS123
D	GLU126
D	MET127
D	HIS287
D	HOH480
D	HOH556

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 430

Chain	Residue
C	ASN44
C	MET45
C	PHE46
C	LYS49
C	HOH542
D	GLU56

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	BINDING:

Chain	Residue	Details
A	ARG20
B	ARG399
C	ARG20
C	TYR74
C	TYR142
C	ASN202
C	ARG399
D	ARG20
D	TYR74
D	TYR142
D	ASN202
A	TYR74
D	ARG399
A	TYR142
A	ASN202
A	ARG399
B	ARG20
B	TYR74
B	TYR142
B	ASN202

site_id	SWS_FT_FI2
Number of Residues	12
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:Q9WVM8

Chain	Residue	Details
A	LYS69
D	LYS69
D	LYS179
D	LYS422
A	LYS179
A	LYS422
B	LYS69
B	LYS179
B	LYS422
C	LYS69
C	LYS179
C	LYS422

site_id	SWS_FT_FI3
Number of Residues	12
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:Q9WVM8

Chain	Residue	Details
A	LLP263
D	LLP263
D	LYS339
D	LYS367
A	LYS339
A	LYS367
B	LLP263
B	LYS339
B	LYS367
C	LLP263
C	LYS339
C	LYS367

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
A	TYR142
A	ASP230

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
B	TYR142
B	ASP230

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
C	TYR142
C	ASP230

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
D	TYR142
D	ASP230

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