Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1JDS

5'-DEOXY-5'-METHYLTHIOADENOSINE PHOSPHORYLASE COMPLEX WITH PHOSPHATE (SPACE GROUP P21)

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	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	0017061	molecular_function	S-methyl-5-thioadenosine phosphorylase activity
B	0003824	molecular_function	catalytic activity
B	0004731	molecular_function	purine-nucleoside phosphorylase activity
B	0005829	cellular_component	cytosol
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	0017061	molecular_function	S-methyl-5-thioadenosine phosphorylase activity
C	0003824	molecular_function	catalytic activity
C	0004731	molecular_function	purine-nucleoside phosphorylase activity
C	0005829	cellular_component	cytosol
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	0017061	molecular_function	S-methyl-5-thioadenosine phosphorylase activity
D	0003824	molecular_function	catalytic activity
D	0004731	molecular_function	purine-nucleoside phosphorylase activity
D	0005829	cellular_component	cytosol
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	0017061	molecular_function	S-methyl-5-thioadenosine phosphorylase activity
E	0003824	molecular_function	catalytic activity
E	0004731	molecular_function	purine-nucleoside phosphorylase activity
E	0005829	cellular_component	cytosol
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	0017061	molecular_function	S-methyl-5-thioadenosine phosphorylase activity
F	0003824	molecular_function	catalytic activity
F	0004731	molecular_function	purine-nucleoside phosphorylase activity
F	0005829	cellular_component	cytosol
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	0017061	molecular_function	S-methyl-5-thioadenosine phosphorylase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 A 1250

Chain	Residue
A	GLY21
A	ARG25
A	ARG86
A	GLY88
A	THR89
A	HOH607
A	TRS1270
D	ARG43

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 B 2250

Chain	Residue
B	ARG25
B	ARG86
B	GLY88
B	THR89
B	HOH599
B	TRS2270
C	ARG43
B	GLY21

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 C 3250

Chain	Residue
B	ARG43
C	GLY21
C	ARG25
C	ARG86
C	GLY88
C	THR89
C	HOH593
C	TRS3270

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 D 4250

Chain	Residue
A	ARG43
D	GLY21
D	ARG25
D	ARG86
D	GLY88
D	THR89
D	HOH604
D	TRS4270

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 E 5250

Chain	Residue
E	GLY21
E	ARG25
E	ARG86
E	GLY88
E	THR89
E	HOH595
E	TRS5270
F	ARG43

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 F 6250

Chain	Residue
E	ARG43
F	GLY21
F	ARG25
F	ARG86
F	GLY88
F	THR89
F	HOH594
F	TRS6270

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TRS A 1270

Chain	Residue
A	ARG86
A	THR89
A	GLU180
A	MET181
A	GLU182
A	PO41250
D	HIS5
D	ARG43

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRS B 2270

Chain	Residue
B	ARG86
B	THR89
B	GLU180
B	MET181
B	GLU182
B	PO42250
C	HIS5

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRS C 3270

Chain	Residue
B	HIS5
C	ARG86
C	THR89
C	GLU180
C	MET181
C	GLU182
C	PO43250

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRS D 4270

Chain	Residue
A	HIS5
D	ARG86
D	THR89
D	GLU180
D	MET181
D	GLU182
D	PO44250

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRS E 5270

Chain	Residue
E	ARG86
E	THR89
E	GLU180
E	MET181
E	GLU182
E	PO45250
F	HIS5

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRS F 6270

Chain	Residue
E	HIS5
F	ARG86
F	THR89
F	GLU180
F	MET181
F	GLU182
F	PO46250

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	THR61-LEU76

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11489901","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	30
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"11489901","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JDS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1JE0","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11489901","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JE0","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"11489901","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	12
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"11489901","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JDT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1JE1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1cg6

Chain	Residue	Details
A	LEU207
A	ASP205

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1cg6

Chain	Residue	Details
B	LEU207
B	ASP205

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1cg6

Chain	Residue	Details
C	LEU207
C	ASP205

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1cg6

Chain	Residue	Details
D	LEU207
D	ASP205

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1cg6

Chain	Residue	Details
E	LEU207
E	ASP205

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1cg6

Chain	Residue	Details
F	LEU207
F	ASP205

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)