6MFB

Crystal structure of 3-hydroxykynurenine transaminase from Aedes aegypti

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004760	molecular_function	serine-pyruvate transaminase activity
A	0005777	cellular_component	peroxisome
A	0008453	molecular_function	alanine-glyoxylate transaminase activity
A	0008483	molecular_function	transaminase activity
A	0009436	biological_process	glyoxylate catabolic process
A	0016740	molecular_function	transferase activity
A	0019265	biological_process	glycine biosynthetic process, by transamination of glyoxylate
A	0036137	molecular_function	kynurenine aminotransferase activity
A	0047315	molecular_function	kynurenine-glyoxylate transaminase activity
A	0097053	biological_process	L-kynurenine catabolic process
B	0004760	molecular_function	serine-pyruvate transaminase activity
B	0005777	cellular_component	peroxisome
B	0008453	molecular_function	alanine-glyoxylate transaminase activity
B	0008483	molecular_function	transaminase activity
B	0009436	biological_process	glyoxylate catabolic process
B	0016740	molecular_function	transferase activity
B	0019265	biological_process	glycine biosynthetic process, by transamination of glyoxylate
B	0036137	molecular_function	kynurenine aminotransferase activity
B	0047315	molecular_function	kynurenine-glyoxylate transaminase activity
B	0097053	biological_process	L-kynurenine catabolic process
C	0004760	molecular_function	serine-pyruvate transaminase activity
C	0005777	cellular_component	peroxisome
C	0008453	molecular_function	alanine-glyoxylate transaminase activity
C	0008483	molecular_function	transaminase activity
C	0009436	biological_process	glyoxylate catabolic process
C	0016740	molecular_function	transferase activity
C	0019265	biological_process	glycine biosynthetic process, by transamination of glyoxylate
C	0036137	molecular_function	kynurenine aminotransferase activity
C	0047315	molecular_function	kynurenine-glyoxylate transaminase activity
C	0097053	biological_process	L-kynurenine catabolic process
D	0004760	molecular_function	serine-pyruvate transaminase activity
D	0005777	cellular_component	peroxisome
D	0008453	molecular_function	alanine-glyoxylate transaminase activity
D	0008483	molecular_function	transaminase activity
D	0009436	biological_process	glyoxylate catabolic process
D	0016740	molecular_function	transferase activity
D	0019265	biological_process	glycine biosynthetic process, by transamination of glyoxylate
D	0036137	molecular_function	kynurenine aminotransferase activity
D	0047315	molecular_function	kynurenine-glyoxylate transaminase activity
D	0097053	biological_process	L-kynurenine catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue PLP A 401

Chain	Residue
A	SER77
A	LYS205
B	TYR256
B	HIS258
B	THR259
A	ALA78
A	HIS79
A	TRP104
A	GLY152
A	SER154
A	ASP179
A	VAL181
A	GLN204

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: in other chain => ECO:0000269|Ref.4, ECO:0007744|PDB:6MFB

Chain	Residue	Details
A	SER77
A	GLN204
C	SER77
C	GLN204
B	SER77
B	GLN204
D	SER77
D	GLN204

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q7PRG3

Chain	Residue	Details
B	SER154
B	ARG356
D	SER154
D	ARG356
A	SER154
A	ARG356
C	SER154
C	ARG356

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site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|Ref.4, ECO:0007744|PDB:6MFB

Chain	Residue	Details
A	TYR256
A	THR259
C	TYR256
C	THR259
B	TYR256
B	THR259
D	TYR256
D	THR259

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site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|PIRSR:PIRSR000524-50, ECO:0000269|Ref.4, ECO:0007744|PDB:6MFB

Chain	Residue	Details
A	LYS205
C	LYS205
B	LYS205
D	LYS205

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