6YMH

X-ray structure of the K72I, Y129F, R133L, H199A quadruple mutant of PNP-oxidase from E. coli in complex with PLP

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
AAA	0004733	molecular_function	pyridoxamine phosphate oxidase activity
AAA	0005829	cellular_component	cytosol
AAA	0006725	biological_process	obsolete cellular aromatic compound metabolic process
AAA	0008615	biological_process	pyridoxine biosynthetic process
AAA	0010181	molecular_function	FMN binding
AAA	0016491	molecular_function	oxidoreductase activity
AAA	0030170	molecular_function	pyridoxal phosphate binding
AAA	0032991	cellular_component	protein-containing complex
AAA	0036001	biological_process	'de novo' pyridoxal 5'-phosphate biosynthetic process
AAA	0042301	molecular_function	phosphate ion binding
AAA	0042803	molecular_function	protein homodimerization activity
AAA	0042816	biological_process	vitamin B6 metabolic process
AAA	0042823	biological_process	pyridoxal phosphate biosynthetic process
AAA	1901615	biological_process	organic hydroxy compound metabolic process
AAA	1902444	molecular_function	riboflavin binding
BBB	0004733	molecular_function	pyridoxamine phosphate oxidase activity
BBB	0005829	cellular_component	cytosol
BBB	0006725	biological_process	obsolete cellular aromatic compound metabolic process
BBB	0008615	biological_process	pyridoxine biosynthetic process
BBB	0010181	molecular_function	FMN binding
BBB	0016491	molecular_function	oxidoreductase activity
BBB	0030170	molecular_function	pyridoxal phosphate binding
BBB	0032991	cellular_component	protein-containing complex
BBB	0036001	biological_process	'de novo' pyridoxal 5'-phosphate biosynthetic process
BBB	0042301	molecular_function	phosphate ion binding
BBB	0042803	molecular_function	protein homodimerization activity
BBB	0042816	biological_process	vitamin B6 metabolic process
BBB	0042823	biological_process	pyridoxal phosphate biosynthetic process
BBB	1901615	biological_process	organic hydroxy compound metabolic process
BBB	1902444	molecular_function	riboflavin binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:11786019

Chain	Residue	Details
AAA	ARG14
AAA	ARG197
BBB	ARG14
BBB	ARG197

---

site_id	SWS_FT_FI2
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269|PubMed:10903950, ECO:0000269|PubMed:11453690, ECO:0000269|PubMed:15858270

Chain	Residue	Details
BBB	LYS89
BBB	GLN146
AAA	GLN146
BBB	ARG67
BBB	TYR82
BBB	ARG88
AAA	ARG67
AAA	TYR82
AAA	ARG88
AAA	LYS89

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:11453690

Chain	Residue	Details
BBB	ILE72
BBB	PHE129
BBB	LEU133
BBB	SER137
AAA	ILE72
AAA	PHE129
AAA	LEU133
AAA	SER137

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:11786019, ECO:0000269|PubMed:15858270

Chain	Residue	Details
AAA	GLN111
AAA	ARG201
BBB	GLN111
BBB	ARG201

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:15858270

Chain	Residue	Details
AAA	TRP191
BBB	TRP191

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	1
Details	M-CSA 677

Chain	Residue	Details
AAA	ARG197	steric role

---

site_id	MCSA2
Number of Residues	1
Details	M-CSA 677

Chain	Residue	Details
BBB	ARG197	steric role

---