Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5MX6

Crystal structure of H. pylori purine nucleoside phosphorylase from clinical isolate HpPNP-2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004731	molecular_function	purine-nucleoside phosphorylase activity
A	0005829	cellular_component	cytosol
A	0006139	biological_process	nucleobase-containing compound metabolic process
A	0006152	biological_process	purine nucleoside catabolic process
A	0009116	biological_process	nucleoside metabolic process
A	0009164	biological_process	nucleoside catabolic process
A	0016757	molecular_function	glycosyltransferase activity
A	0016763	molecular_function	pentosyltransferase activity
B	0003824	molecular_function	catalytic activity
B	0004731	molecular_function	purine-nucleoside phosphorylase activity
B	0005829	cellular_component	cytosol
B	0006139	biological_process	nucleobase-containing compound metabolic process
B	0006152	biological_process	purine nucleoside catabolic process
B	0009116	biological_process	nucleoside metabolic process
B	0009164	biological_process	nucleoside catabolic process
B	0016757	molecular_function	glycosyltransferase activity
B	0016763	molecular_function	pentosyltransferase activity
C	0003824	molecular_function	catalytic activity
C	0004731	molecular_function	purine-nucleoside phosphorylase activity
C	0005829	cellular_component	cytosol
C	0006139	biological_process	nucleobase-containing compound metabolic process
C	0006152	biological_process	purine nucleoside catabolic process
C	0009116	biological_process	nucleoside metabolic process
C	0009164	biological_process	nucleoside catabolic process
C	0016757	molecular_function	glycosyltransferase activity
C	0016763	molecular_function	pentosyltransferase activity
D	0003824	molecular_function	catalytic activity
D	0004731	molecular_function	purine-nucleoside phosphorylase activity
D	0005829	cellular_component	cytosol
D	0006139	biological_process	nucleobase-containing compound metabolic process
D	0006152	biological_process	purine nucleoside catabolic process
D	0009116	biological_process	nucleoside metabolic process
D	0009164	biological_process	nucleoside catabolic process
D	0016757	molecular_function	glycosyltransferase activity
D	0016763	molecular_function	pentosyltransferase activity
E	0003824	molecular_function	catalytic activity
E	0004731	molecular_function	purine-nucleoside phosphorylase activity
E	0005829	cellular_component	cytosol
E	0006139	biological_process	nucleobase-containing compound metabolic process
E	0006152	biological_process	purine nucleoside catabolic process
E	0009116	biological_process	nucleoside metabolic process
E	0009164	biological_process	nucleoside catabolic process
E	0016757	molecular_function	glycosyltransferase activity
E	0016763	molecular_function	pentosyltransferase activity
F	0003824	molecular_function	catalytic activity
F	0004731	molecular_function	purine-nucleoside phosphorylase activity
F	0005829	cellular_component	cytosol
F	0006139	biological_process	nucleobase-containing compound metabolic process
F	0006152	biological_process	purine nucleoside catabolic process
F	0009116	biological_process	nucleoside metabolic process
F	0009164	biological_process	nucleoside catabolic process
F	0016757	molecular_function	glycosyltransferase activity
F	0016763	molecular_function	pentosyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue SO4 A 301

Chain	Residue
A	CYS19
A	GLY20
A	ARG87
A	GLY89
A	THR90
D	ARG43

site_id	AC2
Number of Residues	8
Details	binding site for residue HPA A 302

Chain	Residue
A	PHE159
A	ILE178
A	GLU179
A	ASP204
A	LEU206
A	THR90
A	CYS91
A	GLY92

site_id	AC3
Number of Residues	4
Details	binding site for residue SO4 A 303

Chain	Residue
A	GLN34
A	ASP35
A	ALA36
A	HOH457

site_id	AC4
Number of Residues	3
Details	binding site for residue ACT A 304

Chain	Residue
A	LYS78
A	GLU191
D	PHE162

site_id	AC5
Number of Residues	11
Details	binding site for residue PEG A 305

Chain	Residue
A	ASN122
A	HOH441
A	HOH454
B	ASN122
C	ASN122
C	HOH416
D	ASN122
E	ASN122
E	HOH417
F	ASN122
F	HOH405

site_id	AC6
Number of Residues	8
Details	binding site for residue SO4 B 301

Chain	Residue
B	CYS19
B	GLY20
B	ASP21
B	ARG87
B	GLY89
B	THR90
B	HOH402
E	ARG43

site_id	AC7
Number of Residues	4
Details	binding site for residue HPA B 302

Chain	Residue
B	THR90
B	GLY92
B	PHE159
B	MET180

site_id	AC8
Number of Residues	2
Details	binding site for residue PEG B 303

Chain	Residue
B	ASN6
B	GLU38

site_id	AC9
Number of Residues	7
Details	binding site for residue PO4 C 301

Chain	Residue
C	GLY20
C	ARG24
C	ARG87
C	GLY89
C	THR90
C	HOH417
F	ARG43

site_id	AD1
Number of Residues	8
Details	binding site for residue HPA C 302

Chain	Residue
C	THR90
C	CYS91
C	GLY92
C	PHE159
C	ILE178
C	GLU179
C	ASP204
C	LEU206

site_id	AD2
Number of Residues	6
Details	binding site for residue SO4 C 303

Chain	Residue
A	TYR138
A	LYS142
C	LEU33
C	GLN34
C	ASP35
C	HOH449

site_id	AD3
Number of Residues	3
Details	binding site for residue PEG C 304

Chain	Residue
C	ASN6
C	GLU38
C	ILE39

site_id	AD4
Number of Residues	8
Details	binding site for residue SO4 D 301

Chain	Residue
A	ARG43
D	GLY20
D	ASP21
D	ARG87
D	GLY89
D	THR90
D	HOH403
D	HOH424

site_id	AD5
Number of Residues	4
Details	binding site for residue HPA D 302

Chain	Residue
D	THR90
D	GLY92
D	LEU206
D	HOH460

site_id	AD6
Number of Residues	5
Details	binding site for residue SO4 D 303

Chain	Residue
C	LYS97
D	LEU33
D	GLN34
D	ASP35
D	HOH402

site_id	AD7
Number of Residues	3
Details	binding site for residue PEG D 304

Chain	Residue
D	ASN6
D	GLU38
D	ILE39

site_id	AD8
Number of Residues	8
Details	binding site for residue SO4 E 301

Chain	Residue
B	ARG43
E	CYS19
E	GLY20
E	ASP21
E	ARG24
E	ARG87
E	GLY89
E	THR90

site_id	AD9
Number of Residues	5
Details	binding site for residue HPA E 302

Chain	Residue
E	GLY92
E	PHE159
E	ILE178
E	LEU206
E	THR90

site_id	AE1
Number of Residues	3
Details	binding site for residue PEG E 303

Chain	Residue
E	ASN6
E	GLU38
E	ILE39

site_id	AE2
Number of Residues	8
Details	binding site for residue SO4 F 301

Chain	Residue
C	ARG43
F	GLY20
F	ASP21
F	ARG24
F	ARG87
F	GLY89
F	THR90
F	HOH402

site_id	AE3
Number of Residues	6
Details	binding site for residue HPA F 302

Chain	Residue
F	THR90
F	CYS91
F	GLY92
F	PHE159
F	LEU206
F	HOH441

site_id	AE4
Number of Residues	4
Details	binding site for residue SO4 F 303

Chain	Residue
A	LYS209
A	HOH413
F	GLN34
F	ASP35

site_id	AE5
Number of Residues	5
Details	binding site for residue ACT F 304

Chain	Residue
C	TYR160
C	SER161
C	PHE162
F	LYS78
F	GLU191

Functional Information from PROSITE/UniProt

site_id	PS01232
Number of Residues	16
Details	PNP_UDP_1 Purine and other phosphorylases family 1 signature. GhGMGiAScTIyvtEL

Chain	Residue	Details
A	GLY61-LEU76

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: Proton donor => ECO:0000255\|HAMAP-Rule:MF_01627

Chain	Residue	Details
A	ASP204
B	ASP204
C	ASP204
D	ASP204
E	ASP204
F	ASP204

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P50389

Chain	Residue	Details
A	HIS4
E	ARG43
F	HIS4
F	ARG43
A	ARG43
B	HIS4
B	ARG43
C	HIS4
C	ARG43
D	HIS4
D	ARG43
E	HIS4

site_id	SWS_FT_FI3
Number of Residues	30
Details	BINDING: in other chain => ECO:0000250\|UniProtKB:P50389

Chain	Residue	Details
A	GLY20
B	SER203
C	GLY20
C	ARG24
C	ARG87
C	GLU179
C	SER203
D	GLY20
D	ARG24
D	ARG87
D	GLU179
A	ARG24
D	SER203
E	GLY20
E	ARG24
E	ARG87
E	GLU179
E	SER203
F	GLY20
F	ARG24
F	ARG87
F	GLU179
A	ARG87
F	SER203
A	GLU179
A	SER203
B	GLY20
B	ARG24
B	ARG87
B	GLU179

site_id	SWS_FT_FI4
Number of Residues	6
Details	SITE: Important for catalytic activity => ECO:0000255\|HAMAP-Rule:MF_01627

Chain	Residue	Details
A	ARG217
B	ARG217
C	ARG217
D	ARG217
E	ARG217
F	ARG217

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)