2ZBT

Crystal structure of pyridoxine biosynthesis protein from Thermus thermophilus HB8

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006520	biological_process	amino acid metabolic 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
B	0006520	biological_process	amino acid metabolic 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
C	0006520	biological_process	amino acid metabolic 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
D	0006520	biological_process	amino acid metabolic 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

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MPD C 901

Chain	Residue
C	ASP27
C	LYS84
C	ASP105
C	GLY216
C	PHE236
C	VAL237
C	GLY238

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MPD D 902

Chain	Residue
D	ASP105
D	GLY216
D	PHE236
D	VAL237
D	GLY238
D	ASP27
D	LYS84

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site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MPD A 903

Chain	Residue
A	ASP27
A	LYS84
A	ASP105
A	GLY216
A	PHE236
A	VAL237
A	GLY238

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site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MPD B 904

Chain	Residue
B	ASP27
B	LYS84
B	ASP105
B	GLY216
B	PHE236
B	VAL237
B	GLY238

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU208-LEU226

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Schiff-base intermediate with D-ribose 5-phosphate => ECO:0000255|HAMAP-Rule:MF_01824

Chain	Residue	Details
A	LYS84
B	LYS84
C	LYS84
D	LYS84

---

site_id	SWS_FT_FI2
Number of Residues	20
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01824

Chain	Residue	Details
A	ASP27
B	GLY238
C	ASP27
C	GLY156
C	ARG168
C	GLY217
C	GLY238
D	ASP27
D	GLY156
D	ARG168
D	GLY217
A	GLY156
D	GLY238
A	ARG168
A	GLY217
A	GLY238
B	ASP27
B	GLY156
B	ARG168
B	GLY217

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