1G79

X-RAY STRUCTURE OF ESCHERICHIA COLI PYRIDOXINE 5'-PHOSPHATE OXIDASE COMPLEXED WITH PYRIDOXAL 5'-PHOSPHATE AT 2.0 A RESOLUTION

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004733	molecular_function	pyridoxamine phosphate oxidase activity
A	0005829	cellular_component	cytosol
A	0008615	biological_process	pyridoxine biosynthetic process
A	0010181	molecular_function	FMN binding
A	0016491	molecular_function	oxidoreductase activity
A	0016638	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors
A	0030170	molecular_function	pyridoxal phosphate binding
A	0032991	cellular_component	protein-containing complex
A	0036001	biological_process	'de novo' pyridoxal 5'-phosphate biosynthetic process
A	0042301	molecular_function	phosphate ion binding
A	0042803	molecular_function	protein homodimerization activity
A	0042816	biological_process	vitamin B6 metabolic process
A	0042823	biological_process	pyridoxal phosphate biosynthetic process
A	1902444	molecular_function	riboflavin binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 A 280

Chain	Residue
A	ARG23
A	ARG24
A	ARG120
A	ALA152
A	ARG153
A	ARG215
A	HOH311
A	HOH341
A	HOH350

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A 290

Chain	Residue
A	SER148
A	ARG149
A	HOH369
A	HOH422

---

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE FMN A 250

Chain	Residue
A	ARG67
A	ILE68
A	VAL69
A	LEU70
A	TYR82
A	THR83
A	SER87
A	ARG88
A	LYS89
A	GLN111
A	GLN146
A	SER147
A	TRP191
A	ARG201
A	PLP260
A	HOH308
A	HOH315
A	HOH330
A	HOH409

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site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PLP A 260

Chain	Residue
A	LYS72
A	TYR129
A	ARG133
A	GLN146
A	ARG197
A	HIS199
A	FMN250
A	HOH368
A	HOH405

---

site_id	AC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP A 270

Chain	Residue
A	ARG25
A	ASP26
A	LEU27
A	ASN84
A	TRP142
A	SER144
A	LYS145
A	LYS159
A	SER176
A	PHE177
A	HOH362
A	HOH373
A	HOH374
A	HOH395
A	HOH415

---

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE BME A 300

Chain	Residue
A	CYS43
A	PRO50

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Functional Information from PROSITE/UniProt

site_id	PS01064
Number of Residues	14
Details	PYRIDOX_OXIDASE Pyridoxamine 5'-phosphate oxidase signature. IEFWQggehRLHDR

Chain	Residue	Details
A	ILE188-ARG201

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10903950","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11453690","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15858270","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11453690","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11786019","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15858270","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15858270","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11786019","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 11786019, 15858270, 12686112

Chain	Residue	Details
A	ARG197

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site_id	MCSA1
Number of Residues	1
Details	M-CSA 677

Chain	Residue	Details
A	ARG197	steric role

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