Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1XE3

Crystal Structure of purine nucleoside phosphorylase DeoD from Bacillus anthracis

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	0016740	molecular_function	transferase activity
A	0016757	molecular_function	glycosyltransferase activity
A	0016763	molecular_function	pentosyltransferase activity
A	0042278	biological_process	purine nucleoside metabolic process
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	0016740	molecular_function	transferase activity
B	0016757	molecular_function	glycosyltransferase activity
B	0016763	molecular_function	pentosyltransferase activity
B	0042278	biological_process	purine nucleoside metabolic process
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	0016740	molecular_function	transferase activity
C	0016757	molecular_function	glycosyltransferase activity
C	0016763	molecular_function	pentosyltransferase activity
C	0042278	biological_process	purine nucleoside metabolic process
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	0016740	molecular_function	transferase activity
D	0016757	molecular_function	glycosyltransferase activity
D	0016763	molecular_function	pentosyltransferase activity
D	0042278	biological_process	purine nucleoside metabolic process
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	0016740	molecular_function	transferase activity
E	0016757	molecular_function	glycosyltransferase activity
E	0016763	molecular_function	pentosyltransferase activity
E	0042278	biological_process	purine nucleoside metabolic process
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	0016740	molecular_function	transferase activity
F	0016757	molecular_function	glycosyltransferase activity
F	0016763	molecular_function	pentosyltransferase activity
F	0042278	biological_process	purine nucleoside metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL B 801

Chain	Residue
B	GLY63
B	MET64
B	HOH809
E	GLY63
E	SER68

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL C 802

Chain	Residue
C	THR220
A	THR219
C	ARG101
C	GLU216
C	ARG217

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL F 803

Chain	Residue
E	THR219
F	ARG101
F	GLU216
F	ARG217
F	THR220

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL D 804

Chain	Residue
B	ARG101
B	GLU216
B	ARG217
B	THR220
D	THR219

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 805

Chain	Residue
A	SER68
D	GLY63
D	MET64

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL C 806

Chain	Residue
C	SER113
C	ASN114
C	MET115
C	ASN116
C	ARG117
E	ASP124

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY61-LEU76

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01627","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P50389","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	48
Details	Binding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P50389","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Site: {"description":"Important for catalytic activity","evidences":[{"source":"HAMAP-Rule","id":"MF_01627","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1a69

Chain	Residue	Details
A	ASP204
A	ARG217

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1a69

Chain	Residue	Details
D	ASP204
D	GLU210

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1a69

Chain	Residue	Details
E	ASP204
E	GLU210

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1a69

Chain	Residue	Details
F	ASP204
F	GLU210

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1a69

Chain	Residue	Details
B	ASP204
B	ARG217

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1a69

Chain	Residue	Details
C	ASP204
C	ARG217

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1a69

Chain	Residue	Details
D	ASP204
D	ARG217

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1a69

Chain	Residue	Details
E	ASP204
E	ARG217

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1a69

Chain	Residue	Details
F	ASP204
F	ARG217

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1a69

Chain	Residue	Details
A	ASP204
A	GLU210

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1a69

Chain	Residue	Details
B	ASP204
B	GLU210

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1a69

Chain	Residue	Details
C	ASP204
C	GLU210

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