Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4L6I

Methylthioadenosine phosphorylase from Schistosoma mansoni in complex with adenine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006166	biological_process	purine ribonucleoside salvage
A	0009116	biological_process	nucleoside metabolic 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
A	0019509	biological_process	L-methionine salvage from methylthioadenosine
B	0003824	molecular_function	catalytic activity
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006166	biological_process	purine ribonucleoside salvage
B	0009116	biological_process	nucleoside metabolic 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
B	0019509	biological_process	L-methionine salvage from methylthioadenosine
C	0003824	molecular_function	catalytic activity
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006166	biological_process	purine ribonucleoside salvage
C	0009116	biological_process	nucleoside metabolic 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
C	0019509	biological_process	L-methionine salvage from methylthioadenosine
D	0003824	molecular_function	catalytic activity
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006166	biological_process	purine ribonucleoside salvage
D	0009116	biological_process	nucleoside metabolic 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
D	0019509	biological_process	L-methionine salvage from methylthioadenosine
E	0003824	molecular_function	catalytic activity
E	0005634	cellular_component	nucleus
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006166	biological_process	purine ribonucleoside salvage
E	0009116	biological_process	nucleoside metabolic 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
E	0019509	biological_process	L-methionine salvage from methylthioadenosine
F	0003824	molecular_function	catalytic activity
F	0005634	cellular_component	nucleus
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006166	biological_process	purine ribonucleoside salvage
F	0009116	biological_process	nucleoside metabolic 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
F	0019509	biological_process	L-methionine salvage from methylthioadenosine

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ADE A 301

Chain	Residue
A	ALA88
A	HOH416
A	CYS89
A	GLY90
A	VAL204
A	ASN205
A	MET206
A	THR229
A	ASP230
A	ASP232

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ADE B 301

Chain	Residue
B	ALA88
B	CYS89
B	GLY90
B	PHE187
B	VAL204
B	ASN205
B	MET206
B	THR229
B	ASP230
B	ASP232
B	VAL246
B	HOH403

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 B 302

Chain	Residue
B	GLY11
B	SER12
B	ARG54
B	HIS55
B	THR86
B	ASN87
B	ALA88
B	THR207
B	HOH420
B	HOH442

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 C 301

Chain	Residue
C	GLY11
C	SER12
C	ARG54
C	HIS55
C	ASN87
C	ALA88
C	THR207
C	HOH462
C	HOH488

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE ADE D 301

Chain	Residue
D	ALA88
D	CYS89
D	GLY90
D	PHE187
D	ASN205
D	THR229
D	ASP230
D	ASP232
D	HOH404

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ADE E 301

Chain	Residue
E	ALA88
E	CYS89
E	GLY90
E	PHE187
E	VAL204
E	ASN205
E	MET206
E	THR229
E	ASP230
E	ASP232
E	VAL241
E	VAL246
E	HOH403

site_id	AC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 E 302

Chain	Residue
E	GLY11
E	SER12
E	ARG54
E	HIS55
E	THR86
E	ASN87
E	ALA88
E	THR207
E	HOH458
E	HOH488

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 F 301

Chain	Residue
F	GLY11
F	SER12
F	ARG54
F	HIS55
F	ASN87
F	ALA88
F	THR207
F	HOH447
F	HOH478
F	HOH495

Functional Information from PROSITE/UniProt

site_id	PS01240
Number of Residues	41
Details	PNP_MTAP_2 Purine and other phosphorylases family 2 signature. LprhGkgHlIppseVnyrAn.VwAlkdlGcth.ILatNAcGSL

Chain	Residue	Details
A	LEU52-LEU92

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