Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2R2N

The crystal structure of human kynurenine aminotransferase II in complex with kynurenine

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	14
Details	BINDING SITE FOR RESIDUE PMP A 426

Chain	Residue
A	SER117
A	LYS263
A	ARG270
A	HOH572
A	HOH661
B	TYR74
A	GLN118
A	TYR142
A	ASN202
A	ASP230
A	PRO232
A	TYR233
A	SER260
A	SER262

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PMP B 426

Chain	Residue
A	TYR74
B	SER117
B	GLN118
B	TYR142
B	ASN202
B	ASP230
B	PRO232
B	TYR233
B	SER260
B	SER262
B	LYS263
B	ARG270
B	HOH635

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PMP C 426

Chain	Residue
C	SER117
C	GLN118
C	TYR142
C	ASN202
C	ASP230
C	PRO232
C	TYR233
C	SER260
C	SER262
C	LYS263
C	ARG270
C	HOH694
D	TYR74

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PMP D 426

Chain	Residue
C	TYR74
D	GLY116
D	SER117
D	GLN118
D	TYR142
D	ASN202
D	ASP230
D	PRO232
D	TYR233
D	SER260
D	SER262
D	LYS263
D	ARG270
D	HOH667

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE KYN A 427

Chain	Residue
A	ILE19
A	ARG20
A	LEU293
A	HOH515
B	SER143
B	ASN202
B	ARG399

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE KYN C 427

Chain	Residue
C	ILE19
C	ARG20
C	GLY39
C	LEU40
C	TYR74
C	HOH635
D	ASN202
D	ARG399

site_id	AC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE KYN A 428

Chain	Residue
A	TYR142
A	ASN202
A	ARG399
A	HOH661
B	ILE19
B	ARG20
B	GLY39
B	TYR74
B	HOH453
B	HOH731

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE KYN C 428

Chain	Residue
C	ASN202
C	ARG399
C	HOH657
C	HOH703
D	ILE19
D	GLY39
D	LEU40
D	HOH638

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL D 427

Chain	Residue
D	PRO76
D	SER77
D	ALA78
D	GLY79
D	LEU84
D	HOH697
D	HOH726
D	HOH762

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 429

Chain	Residue
C	HOH629
C	HOH702
C	GLU56
C	ASN57
C	HIS318
C	ARG321

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL D 428

Chain	Residue
D	GLU346
D	TRP347
D	HIS348
D	TRP357
D	TYR397
D	HOH535
D	HOH651

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL D 429

Chain	Residue
C	MET45
C	PHE46
C	PRO47
D	GLU56
D	ASN57
D	HIS318
D	ARG321
D	HOH660
D	HOH759

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 430

Chain	Residue
D	SER207
D	LEU208
D	THR209
D	HOH503
D	HOH533
D	HOH555

site_id	BC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL A 429

Chain	Residue
A	PRO43
A	ASN44
A	PHE46
A	PHE48
A	LYS49
A	GLU65
A	MET68
A	LYS69
A	LEU72
A	HOH478
A	HOH532

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	112
Details	Transit peptide: {"description":"Mitochondrion","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	108
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	40
Details	Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	20
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	12
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9WVM8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	12
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9WVM8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
A	TYR142
A	LYS263
A	ASP230

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
B	TYR142
B	LYS263
B	ASP230

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
C	TYR142
C	LYS263
C	ASP230

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
D	TYR142
D	LYS263
D	ASP230

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