3ATH

Crystal structure of Pyrococcus horikoshii kynurenine aminotransferase in complex with four AKGs as substrates and allosteric effectors

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008483	molecular_function	transaminase activity
A	0009058	biological_process	biosynthetic process
A	0030170	molecular_function	pyridoxal phosphate binding
A	1901605	biological_process	alpha-amino acid metabolic process
C	0008483	molecular_function	transaminase activity
C	0009058	biological_process	biosynthetic process
C	0030170	molecular_function	pyridoxal phosphate binding
C	1901605	biological_process	alpha-amino acid metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP A 429

Chain	Residue
A	GLY128
A	SER268
A	LYS269
A	ARG276
A	AKG431
A	HOH437
C	TYR94
A	SER129
A	GLN130
A	TYR154
A	ASN208
A	ASP236
A	PRO238
A	TYR239
A	THR266

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site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE AKG A 430

Chain	Residue
A	TYR115
A	ASP237
A	PRO238
A	TYR239
A	GLY240
A	GLU241
A	TYR263
A	GLY265
A	THR266
A	ILE270
A	TRP279
A	HOH468
A	HOH569

---

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE AKG A 431

Chain	Residue
A	ARG47
A	GLY64
A	TYR154
A	ASN208
A	TYR239
A	PLP429
A	HOH680
A	HOH684
A	HOH685
A	HOH703
C	TYR94

---

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP C 429

Chain	Residue
A	TYR94
C	GLY128
C	SER129
C	GLN130
C	TYR154
C	ASN208
C	ASP236
C	PRO238
C	TYR239
C	THR266
C	SER268
C	LYS269
C	ARG276
C	AKG431
C	HOH449

---

site_id	AC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE AKG C 430

Chain	Residue
C	TYR115
C	ASP237
C	PRO238
C	TYR239
C	GLY240
C	GLU241
C	TYR263
C	GLY265
C	THR266
C	ILE270
C	TRP279
C	HOH451

---

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE AKG C 431

Chain	Residue
A	TYR94
C	GLY64
C	TYR154
C	ASN208
C	PLP429
C	HOH679
C	HOH680
C	HOH682
C	HOH683

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