3O05

Crystal Structure of Yeast Pyridoxal 5-Phosphate Synthase Snz1 Complxed with Substrate PLP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0006520	biological_process	amino acid metabolic process
A	0006543	biological_process	glutamine catabolic process
A	0008615	biological_process	pyridoxine biosynthetic process
A	0016829	molecular_function	lyase activity
A	0016843	molecular_function	amine-lyase activity
A	0036381	molecular_function	pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
A	0042819	biological_process	vitamin B6 biosynthetic process
A	0042823	biological_process	pyridoxal phosphate biosynthetic process
A	1903600	cellular_component	glutaminase complex
B	0005515	molecular_function	protein binding
B	0006520	biological_process	amino acid metabolic process
B	0006543	biological_process	glutamine catabolic process
B	0008615	biological_process	pyridoxine biosynthetic process
B	0016829	molecular_function	lyase activity
B	0016843	molecular_function	amine-lyase activity
B	0036381	molecular_function	pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
B	0042819	biological_process	vitamin B6 biosynthetic process
B	0042823	biological_process	pyridoxal phosphate biosynthetic process
B	1903600	cellular_component	glutaminase complex
C	0005515	molecular_function	protein binding
C	0006520	biological_process	amino acid metabolic process
C	0006543	biological_process	glutamine catabolic process
C	0008615	biological_process	pyridoxine biosynthetic process
C	0016829	molecular_function	lyase activity
C	0016843	molecular_function	amine-lyase activity
C	0036381	molecular_function	pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
C	0042819	biological_process	vitamin B6 biosynthetic process
C	0042823	biological_process	pyridoxal phosphate biosynthetic process
C	1903600	cellular_component	glutaminase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PLP A 1

Chain	Residue
A	GLU104
A	HOH404
A	TRP111
A	HIS114
A	ARG136
A	ARG137
A	LYS148
A	ARG190
A	HOH335
A	HOH384

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site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP B 1

Chain	Residue
B	ILE83
B	GLU104
B	TRP111
B	HIS114
B	LYS129
B	GLU133
B	ARG136
B	ARG137
B	LYS148
B	HOH309
B	HOH354
B	HOH371
B	HOH373
B	HOH379

---

site_id	AC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLP C 1

Chain	Residue
C	GLU104
C	TRP111
C	HIS114
C	LYS129
C	GLU133
C	ARG136
C	ARG137
C	LYS148
C	HOH351
C	HOH353
C	HOH361
C	HOH391

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Functional Information from PROSITE/UniProt

site_id	PS01235
Number of Residues	19
Details	PDXS_SNZ_1 PdxS/SNZ family signature. LPVVNFAAGGVATPADAAL

Chain	Residue	Details
A	LEU205-LEU223

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Schiff-base intermediate with D-ribose 5-phosphate => ECO:0000250|UniProtKB:O59080

Chain	Residue	Details
A	LYS80
B	LYS80
C	LYS80

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site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000250|UniProtKB:O59080

Chain	Residue	Details
A	ASP23
A	GLY235
B	ASP23
B	GLY152
B	GLY214
B	GLY235
C	ASP23
C	GLY152
C	GLY214
C	GLY235
A	GLY152
A	GLY214

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:20919991

Chain	Residue	Details
A	ARG164
B	ARG164
C	ARG164

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