3FEM

Structure of the synthase subunit Pdx1.1 (Snz1) of PLP synthase from Saccharomyces cerevisiae

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	L-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	L-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	L-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
D	0005515	molecular_function	protein binding
D	0006520	biological_process	amino acid metabolic process
D	0006543	biological_process	L-glutamine catabolic process
D	0008615	biological_process	pyridoxine biosynthetic process
D	0016829	molecular_function	lyase activity
D	0016843	molecular_function	amine-lyase activity
D	0036381	molecular_function	pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
D	0042819	biological_process	vitamin B6 biosynthetic process
D	0042823	biological_process	pyridoxal phosphate biosynthetic process
D	1903600	cellular_component	glutaminase complex
E	0005515	molecular_function	protein binding
E	0006520	biological_process	amino acid metabolic process
E	0006543	biological_process	L-glutamine catabolic process
E	0008615	biological_process	pyridoxine biosynthetic process
E	0016829	molecular_function	lyase activity
E	0016843	molecular_function	amine-lyase activity
E	0036381	molecular_function	pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
E	0042819	biological_process	vitamin B6 biosynthetic process
E	0042823	biological_process	pyridoxal phosphate biosynthetic process
E	1903600	cellular_component	glutaminase complex
F	0005515	molecular_function	protein binding
F	0006520	biological_process	amino acid metabolic process
F	0006543	biological_process	L-glutamine catabolic process
F	0008615	biological_process	pyridoxine biosynthetic process
F	0016829	molecular_function	lyase activity
F	0016843	molecular_function	amine-lyase activity
F	0036381	molecular_function	pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
F	0042819	biological_process	vitamin B6 biosynthetic process
F	0042823	biological_process	pyridoxal phosphate biosynthetic process
F	1903600	cellular_component	glutaminase complex

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	6
Details	Active site: {"description":"Schiff-base intermediate with D-ribose 5-phosphate","evidences":[{"source":"UniProtKB","id":"O59080","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"O59080","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20919991","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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